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6WH4

Crystal structure of HTR2A with inverse agonist

Functional Information from GO Data
ChainGOidnamespacecontents
A0004930molecular_functionG protein-coupled receptor activity
A0004993molecular_functionG protein-coupled serotonin receptor activity
A0005506molecular_functioniron ion binding
A0005886cellular_componentplasma membrane
A0007186biological_processG protein-coupled receptor signaling pathway
A0009055molecular_functionelectron transfer activity
A0016020cellular_componentmembrane
A0020037molecular_functionheme binding
A0022900biological_processelectron transport chain
A0042597cellular_componentperiplasmic space
A0046872molecular_functionmetal ion binding
B0004930molecular_functionG protein-coupled receptor activity
B0004993molecular_functionG protein-coupled serotonin receptor activity
B0005506molecular_functioniron ion binding
B0005886cellular_componentplasma membrane
B0007186biological_processG protein-coupled receptor signaling pathway
B0009055molecular_functionelectron transfer activity
B0016020cellular_componentmembrane
B0020037molecular_functionheme binding
B0022900biological_processelectron transport chain
B0042597cellular_componentperiplasmic space
B0046872molecular_functionmetal ion binding
C0004930molecular_functionG protein-coupled receptor activity
C0004993molecular_functionG protein-coupled serotonin receptor activity
C0005506molecular_functioniron ion binding
C0005886cellular_componentplasma membrane
C0007186biological_processG protein-coupled receptor signaling pathway
C0009055molecular_functionelectron transfer activity
C0016020cellular_componentmembrane
C0020037molecular_functionheme binding
C0022900biological_processelectron transport chain
C0042597cellular_componentperiplasmic space
C0046872molecular_functionmetal ion binding
Functional Information from PROSITE/UniProt
site_idPS00237
Number of Residues17
DetailsG_PROTEIN_RECEP_F1_1 G-protein coupled receptors family 1 signature. ASImHLCAISLDRYVaI
ChainResidueDetails
AALA161-ILE177

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBinding site: {"description":"axial binding residue"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues48
DetailsTransmembrane: {"description":"Helical; Name=1","evidences":[{"source":"PubMed","id":"36171289","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7RAN","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues58
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"36171289","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7RAN","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues75
DetailsTransmembrane: {"description":"Helical; Name=2","evidences":[{"source":"PubMed","id":"36171289","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7RAN","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues61
DetailsTopological domain: {"description":"Extracellular","evidences":[{"source":"PubMed","id":"36171289","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7RAN","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues72
DetailsTransmembrane: {"description":"Helical; Name=3","evidences":[{"source":"PubMed","id":"36171289","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7RAN","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues46
DetailsTransmembrane: {"description":"Helical; Name=4","evidences":[{"source":"PubMed","id":"36171289","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7RAN","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues75
DetailsTransmembrane: {"description":"Helical; Name=5","evidences":[{"source":"PubMed","id":"36171289","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7RAN","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues75
DetailsTransmembrane: {"description":"Helical; Name=6","evidences":[{"source":"PubMed","id":"36171289","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7RAN","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues75
DetailsTransmembrane: {"description":"Helical; Name=7","evidences":[{"source":"PubMed","id":"36171289","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7RAN","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues6
DetailsMotif: {"description":"DRY motif; important for ligand-induced conformation changes","evidences":[{"source":"UniProtKB","id":"P41595","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues12
DetailsMotif: {"description":"NPxxY motif; important for ligand-induced conformation changes and signaling","evidences":[{"source":"UniProtKB","id":"P41595","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"35084960","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7WC4","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI14
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"35084960","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"7WC4","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI15
Number of Residues3
DetailsSite: {"description":"Hydrophobic barrier that decreases the speed of ligand binding and dissociation","evidences":[{"source":"PubMed","id":"28129538","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

243911

PDB entries from 2025-10-29

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