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Supriya Shakya Saha
33 articles
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  • . Serotonergic signaling has also been implicated in bronchoconstriction (Hershenson et al. 1995) and the control of rhythmic breathing (Manzke et al. 2010).
  • Serotonergic dysregulation has been linked to numerous psychological conditions, particularly major depressive disorder
  • and memory
  • Within the CNS, 5-HT is involved in the regulation of mood and social cognition (Jenkins et al. 2016), neurogenesis
  • The serotonin transporter (SERT) is responsible for the reuptake of free 5-HT in the synaptic cleft; this is, in fact, the mechanism of action exploited by selective serotonin reuptake inhibitors (SSRIs), typically used as antidepressants or anxiolytic therapy.
  • auto- or paracrine factor, and synthesized by both gut neurons and enterochromaffin cells located in the gastrointestinal system
  • Serotonin acts as a neurotransmitter within the central nervous system (CNS), where it is synthesized by raphe neurons in the brain stem
  • 5-HT receptors are able to exert their influence on several biochemical pathways that are much further downstream
  • Barring the 5-HT3 receptor, which functions as a ligand-gated ion channel (LGIC) (Reeves and Lummis 2002), all other serotonergic receptors mediate their actions via G proteins.
  • 5-Hydroxytryptamine (5-HT), or serotonin, is most commonly known for its role in the pathophysiology of various neuropsychiatric disorders
  • We identified 90 molecules in serotonin-serotonin receptor pathway.
  • Fourteen structurally and functionally distinct receptor subtypes have been identified for serotonin, each of which mediates the neurotransmitter’s effects through a range of downstream signaling molecules and effectors
12 annotations
  • classical paradigm, in which serotonin works by noncovalent interactions with membrane-bound receptors, and creates many new questions about whether serotonin can exert biological activity by covalently attaching to cellular proteins in other organ systems, including the brain.Go to:
  • activation of a subset of platelet
  • serotonin is covalently cross-linked to a variety of adhesion proteins and clotting factors on the platelet cell surface (
  • activates G protein–dependent signaling pathways and stimulates platelet aggregation
  • y also play a role in platelet activation through covalent linkage to small G proteins via tissue transglutaminase
  • SSRIs may actually reduce MIs is intriguing and still awaits prospective testing (26).
  • SSRI treatment may decrease myocardial infarction (MI) risk. Several case-control studies have observed lower MI rates among depressed patients taking SSRIs versus controls
  • platelets from serotonin transporter knockout mice, show decreased aggregation responses (22).
  • Selective serotonin reuptake inhibitors (SSRIs) can increase bleeding time by inhibiting the uptake and storage of platelet serotonin, so caution should be used in patients at high risk for bleeding or on anticoagulants.
  • erotonin is then secreted by the platelet dense granules during platelet activation and plays a role in promoting platelet aggregation and vasoconstriction of surrounding blood vessels, facilitating hemostasis.
  • Platelets have significant vesicular serotonin stores but lack the enzymes to synthesize serotonin (21); instead, they take up serotonin from the plasma via the serotonin transporter. S
  • Serotonin causes vasoconstriction or vasodilation in different vascular beds depending on the particular receptors that are expressed in each vessel wall and surrounding smooth muscle tissue (19). Indeed, activation of 5-HT1B receptors on cerebral blood vessels causes vasodilation, which may partly explain the analgesic effects of the triptan antimigraine drugs (
  • . This principle explains why drugs targeting a specific serotonin receptor nonetheless have effects on multiple behavioral processes (
  • anxiety-like behavior is regulated primarily by 5-HT1A and 5-HT2C receptors, among others (14, 15), but the 5-HT2C receptor regulates not only anxiety but also reward processing, locomotion, appetite, and energy balanc
  • each behavior is regulated by multiple serotonin receptors, each serotonin receptor is expressed in multiple brain regions and likely contributes to the modulation of multiple behavioral processes.
15 annotations
  • of 17 residues of the RBD are in contact with 20 residues of ACE2
  • A total of nine cysteine residues are found in the RBD, eight of which form four pairs of disulfide bonds that are
  • esidues Ser19–Asp615 of the ACE2 N-terminal peptidase domain, one zinc ion, four N-acetyl-β-glucosaminide (NAG) glycans linked to ACE2 Asn90, Asn322 and Asn546 and to RBD Asn343,
  • Thr333–Gly526 of the SARS-CoV-2 RB
  • Specifically, we expressed the SARS-CoV-2 RBD (residues Arg319–Phe541) (Fig. 1a, b) and the N-terminal peptidase domain of ACE2 (residues Ser19–Asp615) in Hi5 insect cells and purified them by Ni-NTA affinity purification and gel filtration
  • Serial dilutions of the SARS-CoV RBD and SARS-CoV-2 RBD were flowed through with a concentration ranging from 62.5 to 1.9 nM. The resulting data were fit to a 1:1 binding model using Biacore Evaluation Software
  • Final Ramachandran statistics: 96.44% favoured, 3.56% allowed and 0.00% outliers for the final structure.
  • structure was determined using the molecular replacement method with PHASER in the CCP4 suit
  • the RBD is the important region for receptor binding, antibodies that target the conserved epitopes in the RBD will also present a great potential for developing highly potent cross-reactive therapeutic agents against diverse coronavirus species, including SARS-CoV-2.
  • 16 residue changes in the SARS-CoV-2 RBD among 25 epitope positions of
  • By mapping these epitope residues onto the sequence of SARS-CoV RBD aligned with the sequence of SARS-CoV-2 RBD
  • where exactly the epitope of CR3022 on the RBDs of SARS-CoV or SARS-CoV-2 is located.
  • the equilibrium dissociation constant
  • may have important roles in the binding of
  • reside in the Asn90-
  • e involvement of multiple
  • tyrosine residues that form hydrogen-bonding interaction
  • K417 and V404 positions of SARS-CoV-2
  • charged patch on the SARS-CoV-2 RBD
  • Lys417 t
  • Outside the RBM, there is a unique ACE2-interacting residue (Lys417) in SARS-CoV-2, which forms salt-bridge interactions with Asp30 of ACE2
  • At the Gln493/Asn479 position, Gln493 of SARS-CoV-2 interacts with Lys31, His34 and Glu35 of ACE2 and forms a hydrogen bond with Glu35; Asn479 of SARS-CoV interacts with only His34 of ACE2 (
  • At the Phe486/Leu472 position, Phe486 of SARS-CoV-2 interacts with Gln24, Leu79, Met82 and Tyr83 of ACE2
  • at which Gln498 of SARS-CoV-2 and Tyr484 of SARS-CoV both interact with Asp38, Tyr41, Gln42, Leu45 and Lys353 of ACE2
  • Gln498/Tyr484 location
  • , 8 have the identical residues between the two RBDs, inc
  • structure-guided sequence alignment and mapped them to their respective sequen
  • To compare the ACE2-interacting residues on the SARS-CoV-2 and SARS-CoV RBD
  • , 17 residues are shared between both interactions and most of the contacting residues are located at the N-terminal helix
  • N-terminal helix of ACE2 by the outer surface
  • binding site between them
  • f ACE2 has two lobes
  • forming the peptide substrate
  • ), which help to stabilize the β sheet structure (Fig. 1c); the remaining pair (Cys480–Cys488) connects the loops in the distal end of the RBM
  • , three are in the core
  • crystallography.
  • d the structure of the SARS-CoV-2 RBD–ACE2 complex using X-ray
  • Previous cryo-electron microscopy studies of the SARS-CoV spike protein and its interaction with the cell receptor ACE2 have shown that receptor binding induces the dissociation of the S1 with ACE2, prompting the S2 to transit from a metastable pre-fusion to a more-stable post-fusion state that is essential for membrane fusion
38 annotations
  • r Lys353 in binding other than stabilizing the internal configuration of ACE2 by forming an ion pair with Asp38.
  • simulations show that Asn501 makes a second hydrogen bond to the main-chain oxygen of Gly352 of ACE2
  • as long as they are hydrophobic in nature, would not ma
  • nonspecific, hydrophobic aggregation is key to initiate contact between ACE2 and RBD
  • no specific side-chain contacts from the receptor ACE2, except the methyl group of Thr27.
  • crystal structures and from MD simulation
  • Asp30 to Glu30 in the receptor could also effectively accommodate ion-pair interactions
  • an ion pair across the otherwise hydrophobic interface in the central region of the binary complex
  • Val404s-to-Lys417 mutation
  • crystal and cryo-EM structures and amino acid sequences provided important insights
  • double mutation of both Lys439s and Asp480s, as in the RBD of SARS-CoV-2, to Leu452 and Ser494, respectively, may not necessarily yield a net destabilizing contribution to binding.
  • counterbalance the stabilizing effect of ion pairing
  • Asp480s also forms a tight salt bridge with Lys439s, which is only 3.6 Å from Arg162.
  • . Indeed, single-site mutation of either Asp480sAla or Asp480sGly abolishes binding activity of 80R for the RBD of SARS-CoV
  • light and heavy chains
  • stabilizing since it disrupts an internal salt bridge of 80R (Arg156–Asp202), and Asp202 is only 4 Å away from Glu484.
  • along with a new ion pair between Glu484 and Arg156(H) thanks to the Pro470s→Glu484 mutation.
  • crystal structure [Protein Data Bank (PDB)
  • , Asp355 itself is involved in an internal (among residues of ACE2) salt bridge with Arg357 as well as a hydrogen bond from Tyr41 of the receptor,
  • Asp355 on the β-sheet/turn of ACE2 receives a hydrogen bond from Thr500 at the tip of the binding loop
  • Gly502–Lys353 pair is preserved in the SARS-CoV complex, but the other hydrogen bond is absent as a result of the amino acid variation of Thr487s
  • Asn501 and the backbone of Gly502 each donates a hydrogen bond to the main-chain oxygen atoms of Gly352 and Lys353, respectively.
  • anchoring the RBD in a groove formed between the turn of an antiparallel β-sheet and the long N-terminal helix of ACE2.
  • extensive hydrogen-bonding network
  • does not form specific contacts with ACE2 except remote interactions with the Lys31–Asp35 salt bridge on the N-terminal helix.
  • ACE2
  • ” Lys31, of
  • Gln493(Asn479s), which has been recognized as a key residue whose mutation may be associated with the possible civet (from Arg or Lys)-to-human transmission,
  • demonstrating its significant role in ACE2 binding.
  • Val→Lys displacement enhances RBD binding to ACE2
  • in the RBD–ACE2 complex between SARS-CoV-2 and SARS-CoV is the Val404s-to-Lys417 transition at the apex of the interfacial arch, resulting in an ion pair with Asp30 in the 2019 novel coronavirus.
  • significant role to anchor the dimer interface in the RBD–ACE2 complexes.
  • hydrophobic contacts
  • although these two sets of hydrophobic residues are quite different in the two RBDs, they form the same type of physical interactions in both complex structures.
  • , from Tyr442s, Leu443s, F460s, and Pro462s
  • other four hydrophobic residues have been mutated in SARS-CoV-2,
  • Tyr489 is retained from the SARS-CoV sequence,
  • including Leu455, Phe456, Tyr473, Ala475, and Tyr489, ending with the methyl group of Thr27 of ACE2 tucked in the pocket of the last four residues
  • The interfacial interactions in the central region across the N-terminal helix of ACE2 are dominated by hydrophobic contacts both within the RBM of SARS-CoV-2 itself and across the interface with the recepto
  • It is interesting to note that the Leu472s→Phe mutation has been identified previously in a set of five amino acid variations of the original
  • esidue Leu472s in SARS-CoV is, however, found to point outward, rather than seating in the pocket in the dynamic trajectories, also observed in crystallograph
  • Tyr83 also donates a hydrogen bond to Asn487
  • N-terminal end of ACE2 is the hydrophobic contact of Phe486, situated in a pocket fenced by Leu79, Met82, and Tyr83 of ACE2.
  • The interface between ACE2 and RBD may be roughly divided into hydrophobic and hydrogen-bonding halves.
  • e three key binding contact regions
  • etween SARS-CoV-2 and S
  • structural origin that governs RBD–ACE2 binding and affinity difference between SARS-CoV-2 and SARS-CoV,
  • Hydrophobic Contacts Play a Central Role in Anchoring RBD to Its Receptor.
  • uncertainties in side-chain conformation found in different crystal structures (Gln498 and Asn501) and residues in the central region of RBM, including Lys417 and Tyr453
  • e MD simulations, which are as representative as any other structures of the trajectory, with the four crystal and cryogenic electron microscopy (cryo-EM) structures of SAR2-CoV-2 that have been solved
  • . Consistent with electrostatic potential complementarity and structural details (discussed below), the observed conformation shift may be attributed to the formation of a salt bridge between Asp30 of ACE2 and Lys417 across the binding groove, along with strengthened loop-anchoring interactions at the bases of the binding interface.
  • receptor binding motif
  • RBD is structurally divided into a core region, consisting of five antiparallel strands of β-sheet, which is relatively conserved (87.4% sequence identity), and a more variable
  • A key mutation from a hydrophobic residue in the SARS-CoV sequence to Lys417 in SARS-CoV-2 creates a salt bridge across the central hydrophobic contact region, which along with polar residue mutations results in greater electrostatic complementarity than that of the SARS-CoV complex.
54 annotations
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Research and EducationAdvanced Search|Browse Annotations Navigation TabsStructure Summary3D ViewAnnotationsExperimentSequence7A97 Display Files FASTA SequencePDB FormatPDB Format (Header)mmCIF FormatmmCIF Format (Header) Download Files FASTA SequencePDB FormatPDB Format (gz)PDBx/mmCIF FormatPDBx/mmCIF Format (gz)PDBML/XML Format (gz)Biological Assembly 1Download EM MapValidation Full PDFValidation XML SARS-CoV-2 Spike Glycoprotein with 2 ACE2 Bounddiv#help { text-align: right; } div#help a { text-decoration: none; } div#help span.glyphicon-new-window { font-size: 10px; margin-left: 10px; } Help Sequence of7A97 | SARS-CoV-2 Spike Glycoprotein with 2 ACE2 Bound1: Spike glycoprotein2: Angiotensin-converting enzyme 2ABC     ​M​​G​​I​​L​​P​​S​​P​​G​​M​​P​     ​A​​L​​L​​S​​L​​V​​S​​L​​L​​S​     ​V​​L​​L​​M​​G​​C​​V​​A​​E​​T​     ​G​​M​​F​​V​​F​​L​​V​​L​​L​​P​     ​L​​V​​S​​S​​Q​​C​​V​​N​​L​​T​20   ​T​​R​​T​​Q​​L​​P​​P​​A​​Y​​T​30   ​N​​S​​F​​T​​R​​G​​V​​Y​​Y​​P​40   ​D​​K​​V​​F​​R​​S​​S​​V​​L​​H​50   ​S​​T​​Q​​D​​L​​F​​L​​P​​F​​F​60   ​S​​N​​V​​T​​W​​F​​H​​A​​I​​H​70   ​V​​S​​G​​T​​N​​G​​T​​K​​R​​F​80   ​D​​N​​P​​V​​L​​P​​F​​N​​D​​G​90   ​V​​Y​​F​​A​​S​​T​​E​​K​​S​​N​100  ​I​​I​​R​​G​​W​​I​​F​​G​​T​​T​110  ​L​​D​​S​​K​​T​​Q​​S​​L​​L​​I​120  ​V​​N​​N​​A​​T​​N​​V​​V​​I​​K​130  ​V​​C​​E​​F​​Q​​F​​C​​N​​D​​P​140  ​F​​L​​G​​V​​Y​​Y​​H​​K​​N​​N​150  ​K​​S​​W​​M​​E​​S​​E​​F​​R​​V​160  ​Y​​S​​S​​A​​N​​N​​C​​T​​F​​E​170  ​Y​​V​​S​​Q​​P​​F​​L​​M​​D​​L​180  ​E​​G​​K​​Q​​G​​N​​F​​K​​N​​L​190  ​R​​E​​F​​V​​F​​K​​N​​I​​D​​G​200  ​Y​​F​​K​​I​​Y​​S​​K​​H​​T​​P​210  ​I​​N​​L​​V​​R​​D​​L​​P​​Q​​G​220  ​F​​S​​A​​L​​E​​P​​L​​V​​D​​L​230  ​P​​I​​G​​I​​N​​I​​T​​R​​F​​Q​240  ​T​​L​​L​​A​​L​​H​​R​​S​​Y​​L​250  ​T​​P​​G​​D​​S​​S​​S​​G​​W​​T​260  ​A​​G​​A​​A​​A​​Y​​Y​​V​​G​​Y​270  ​L​​Q​​P​​R​​T​​F​​L​​L​​K​​Y​280  ​N​​E​​N​​G​​T​​I​​T​​D​​A​​V​290  ​D​​C​​A​​L​​D​​P​​L​​S​​E​​T​300  ​K​​C​​T​​L​​K​​S​​F​​T​​V​​E​310  ​K​​G​​I​​Y​​Q​​T​​S​​N​​F​​R​320  ​V​​Q​​P​​T​​E​​S​​I​​V​​R​​F​330  ​P​​N​​I​​T​​N​​L​​C​​P​​F​​G​340  ​E​​V​​F​​N​​A​​T​​R​​F​​A​​S​350  ​V​​Y​​A​​W​​N​​R​​K​​R​​I​​S​360  ​N​​C​​V​​A​​D​​Y​​S​​V​​L​​Y​370  ​N​​S​​A​​S​​F​​S​​T​​F​​K​​C​380  ​Y​​G​​V​​S​​P​​T​​K​​L​​N​​D​390  ​L​​C​​F​​T​​N​​V​​Y​​A​​D​​S​400  ​F​​V​​I​​R​​G​​D​​E​​V​​R​​Q​410  ​I​​A​​P​​G​​Q​​T​​G​​K​​I​​A​420  ​D​​Y​​N​​Y​​K​​L​​P​​D​​D​​F​430  ​T​​G​​C​​V​​I​​A​​W​​N​​S​​N​440  ​N​​L​​D​​S​​K​​V​​G​​G​​N​​Y​450  ​N​​Y​​L​​Y​​R​​L​​F​​R​​K​​S​460  ​N​​L​​K​​P​​F​​E​​R​​D​​I​​S​470  ​T​​E​​I​​Y​​Q​​A​​G​​S​​T​​P​480  ​C​​N​​G​​V​​E​​G​​F​​N​​C​​Y​490  ​F​​P​​L​​Q​​S​​Y​​G​​F​​Q​​P​500  ​T​​N​​G​​V​​G​​Y​​Q​​P​​Y​​R​510  ​V​​V​​V​​L​​S​​F​​E​​L​​L​​H​520  ​A​​P​​A​​T​​V​​C​​G​​P​​K​​K​530  ​S​​T​​N​​L​​V​​K​​N​​K​​C​​V​540  ​N​​F​​N​​F​​N​​G​​L​​T​​G​​T​550  ​G​​V​​L​​T​​E​​S​​N​​K​​K​​F​560  ​L​​P​​F​​Q​​Q​​F​​G​​R​​D​​I​570  ​A​​D​​T​​T​​D​​A​​V​​R​​D​​P​580  ​Q​​T​​L​​E​​I​​L​​D​​I​​T​​P​590  ​C​​S​​F​​G​​G​​V​​S​​V​​I​​T​600  ​P​​G​​T​​N​​T​​S​​N​​Q​​V​​A​610  ​V​​L​​Y​​Q​​D​​V​​N​​C​​T​​E​     ​V​​P​​V​​A​​I​​H​​A​​D​​Q​​L​     ​T​​P​​T​​W​​R​​V​​Y​​S​​T​​G​     ​S​​N​​V​​F​​Q​​T​​R​​A​​G​​C​650  ​L​​I​​G​​A​​E​​H​​V​​N​​N​​S​660  ​Y​​E​​C​​D​​I​​P​​I​​G​​A​​G​670  ​I​​C​​A​​S​​Y​​Q​​T​​Q​​T​​N​     ​S​​P​​R​​R​​A​​R​​S​​V​​A​​S​690  ​Q​​S​​I​​I​​A​​Y​​T​​M​​S​​L​700  ​G​​A​​E​​N​​S​​V​​A​​Y​​S​​N​710  ​N​​S​​I​​A​​I​​P​​T​​N​​F​​T​720  ​I​​S​​V​​T​​T​​E​​I​​L​​P​​V​730  ​S​​M​​T​​K​​T​​S​​V​​D​​C​​T​740  ​M​​Y​​I​​C​​G​​D​​S​​T​​E​​C​750  ​S​​N​​L​​L​​L​​Q​​Y​​G​​S​​F​760  ​C​​T​​Q​​L​​N​​R​​A​​L​​T​​G​770  ​I​​A​​V​​E​​Q​​D​​K​​N​​T​​Q​780  ​E​​V​​F​​A​​Q​​V​​K​​Q​​I​​Y​790  ​K​​T​​P​​P​​I​​K​​D​​F​​G​​G​800  ​F​​N​​F​​S​​Q​​I​​L​​P​​D​​P​810  ​S​​K​​P​​S​​K​​R​​S​​F​​I​​E​820  ​D​​L​​L​​F​​N​​K​​V​​T​​L​​A​     ​D​​A​​G​​F​​I​​K​​Q​​Y​​G​​D​     ​C​​L​​G​​D​​I​​A​​A​​R​​D​​L​     ​I​​C​​A​​Q​​K​​F​​N​​G​​L​​T​860  ​V​​L​​P​​P​​L​​L​​T​​D​​E​​M​870  ​I​​A​​Q​​Y​​T​​S​​A​​L​​L​​A​880  ​G​​T​​I​​T​​S​​G​​W​​T​​F​​G​890  ​A​​G​​A​​A​​L​​Q​​I​​P​​F​​A​900  ​M​​Q​​M​​A​​Y​​R​​F​​N​​G​​I​910  ​G​​V​​T​​Q​​N​​V​​L​​Y​​E​​N​920  ​Q​​K​​L​​I​​A​​N​​Q​​F​​N​​S​930  ​A​​I​​G​​K​​I​​Q​​D​​S​​L​​S​940  ​S​​T​​A​​S​​A​​L​​G​​K​​L​​Q​950  ​D​​V​​V​​N​​Q​​N​​A​​Q​​A​​L​960  ​N​​T​​L​​V​​K​​Q​​L​​S​​S​​N​970  ​F​​G​​A​​I​​S​​S​​V​​L​​N​​D​980  ​I​​L​​S​​R​​L​​D​​P​​P​​E​​A​990  ​E​​V​​Q​​I​​D​​R​​L​​I​​T​​G​1000 ​R​​L​​Q​​S​​L​​Q​​T​​Y​​V​​T​1010 ​Q​​Q​​L​​I​​R​​A​​A​​E​​I​​R​1020 ​A​​S​​A​​N​​L​​A​​A​​T​​K​​M​1030 ​S​​E​​C​​V​​L​​G​​Q​​S​​K​​R​1040 ​V​​D​​F​​C​​G​​K​​G​​Y​​H​​L​1050 ​M​​S​​F​​P​​Q​​S​​A​​P​​H​​G​1060 ​V​​V​​F​​L​​H​​V​​T​​Y​​V​​P​1070 ​A​​Q​​E​​K​​N​​F​​T​​T​​A​​P​1080 ​A​​I​​C​​H​​D​​G​​K​​A​​H​​F​1090 ​P​​R​​E​​G​​V​​F​​V​​S​​N​​G​1100 ​T​​H​​W​​F​​V​​T​​Q​​R​​N​​F​1110 ​Y​​E​​P​​Q​​I​​I​​T​​T​​D​​N​1120 ​T​​F​​V​​S​​G​​N​​C​​D​​V​​V​1130 ​I​​G​​I​​V​​N​​N​​T​​V​​Y​​D​1140 ​P​​L​​Q​​P​​E​​L​​D​​S​​F​​K​     ​E​​E​​L​​D​​K​​Y​​F​​K​​N​​H​     ​T​​S​​P​​D​​V​​D​​L​​G​​D​​I​     ​S​​G​​I​​N​​A​​S​​V​​V​​N​​I​     ​Q​​K​​E​​I​​D​​R​​L​​N​​E​​V​     ​A​​K​​N​​L​​N​​E​​S​​L​​I​​D​     ​L​​Q​​E​​L​​G​​K​​Y​​E​​Q​​S​     ​G​​R​​E​​N​​L​​Y​​F​​Q​​G​​G​     ​G​​G​​S​​G​​Y​​I​​P​​E​​A​​P​     ​R​​D​​G​​Q​​A​​Y​​V​​R​​K​​D​     ​G​​E​​W​​V​​L​​L​​S​​T​​F​​L​     ​G​​H​​H​​H​​H​​H​​H​Structure7A97 | SARS-CoV-2 Spike Glycoprotein with 2 ACE2 BoundTypeAssemblyAsm Id1: Author And Software Defined AssemblyNothing FocusedMeasurementsComponents7A97PresetAddPolymerCartoonDensityAssembly Symmetry// handle viewer select function selectViewer() { var val = $("#viewers").val() console.log('val=' + val + ', pdbid=' + pdbid + ', bionumber=' + bionumber + ', viewerType=' + viewerType) if (val === 'molstar') { window.location.href = '/3d-view/' + pdbid } else if (val === 'ngl') { window.location.href = '/3d-view/ngl/' + pdbid } else if (val === 'jsmol') { window.location.href = '/3d-view/jsmol/' + pdbid } } Select a different viewerMol* (Javascript)NGL (WebGL)JSmol (JavaScript)CitationImages created using Mol* should cite the PDB ID, the corresponding structure publication, Mol* (D. Sehnal, A.S. Rose, J. Kovca, S.K. Burley, S. Velankar (2018) Mol*: Towards a common library and tools for web molecular graphics MolVA/EuroVis Proceedings. doi:10.2312/molva.20181103), and RCSB PDB.var viewer = new rcsbMolstar.Viewer('viewer'); if (preset === 'validationReport') { viewer.loadPdbId(pdbid, { kind: 'validation', assemblyId: bionumber }); } else if (preset === 'ligandInteraction') { viewer.loadPdbId(pdbid, { kind: 'feature', assemblyId: bionumber, target: { label_comp_id: sele } }); } else if (preset === 'oligoInteraction') { viewer.loadPdbId(pdbid, { kind: 'feature', assemblyId: bionumber, target: { label_asym_id: sele } }); } else if (preset === 'electronDensityMaps') { viewer.loadPdbId(pdbid, { kind: 'density', assemblyId: bionumber }); } else if (preset === 'symmetry') { viewer.loadPdbId(pdbid, { kind: 'symmetry', assemblyId: bionumber, symmetryIndex: parseInt(sele) }); } else { viewer.loadPdbId(pdbid, { kind: 'standard', assemblyId: bionumber }); }AboutAbout UsCiting UsPublicationsTeamCareersUsage & PrivacyHelpContact UsHelp TopicsWebsite FAQGlossaryRCSB PartnersNucleic Acid DatabasewwPDB PartnersRCSB PDBPDBePDBjBMRBRCSB PDB (citation) is hosted byRCSB PDB is a member of theRCSB PDB is funded by the National Science Foundation (DBI-1832184), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM133198.
2 annotations