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5WS3

Crystal structures of human orexin 2 receptor bound to the selective antagonist EMPA determined by serial femtosecond crystallography at SACLA

Functional Information from GO Data
ChainGOidnamespacecontents
A0004930molecular_functionG protein-coupled receptor activity
A0007186biological_processG protein-coupled receptor signaling pathway
A0007631biological_processfeeding behavior
A0016020cellular_componentmembrane
A0016499molecular_functionorexin receptor activity
Functional Information from PDB Data
site_idAC1
Number of Residues11
Detailsbinding site for residue 7MA A 2001
ChainResidue
ATHR111
AHIS350
ATYR354
APRO131
AGLN134
AGLN187
AGLU212
APHE227
AILE320
ASER321
AASN324

site_idAC2
Number of Residues1
Detailsbinding site for residue OLA A 2002
ChainResidue
AOLA2004

site_idAC3
Number of Residues6
Detailsbinding site for residue OLA A 2003
ChainResidue
AGLU54
ATRP55
AILE62
ALEU150
ATYR154
ALEU238

site_idAC4
Number of Residues1
Detailsbinding site for residue OLA A 2004
ChainResidue
AOLA2002

site_idAC5
Number of Residues6
Detailsbinding site for residue OLA A 2005
ChainResidue
ATYR53
AVAL56
ALEU57
AVAL179
AALA344
ATRP351

site_idAC6
Number of Residues8
Detailsbinding site for residue 1PE A 2006
ChainResidue
ALEU43
ATYR47
ATHR204
ATHR205
ASER1022
ALYS1026
APHE1104
AGLU1107

site_idAC7
Number of Residues4
Detailsbinding site for residue 1PE A 2007
ChainResidue
ACYS210
ALYS327
APHE333
APHE346

Functional Information from PROSITE/UniProt
site_idPS00237
Number of Residues17
DetailsG_PROTEIN_RECEP_F1_1 G-protein coupled receptors family 1 signature. VSVlTLSCIALDRWYaI
ChainResidueDetails
AVAL140-ILE156

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=1","evidences":[{"source":"PubMed","id":"25533960","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues31
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"25533960","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues21
DetailsTransmembrane: {"description":"Helical; Name=2","evidences":[{"source":"PubMed","id":"25533960","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues61
DetailsTopological domain: {"description":"Extracellular","evidences":[{"source":"PubMed","id":"25533960","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues22
DetailsTransmembrane: {"description":"Helical; Name=3","evidences":[{"source":"PubMed","id":"25533960","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=4","evidences":[{"source":"PubMed","id":"25533960","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=5","evidences":[{"source":"PubMed","id":"25533960","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues21
DetailsTransmembrane: {"description":"Helical; Name=6","evidences":[{"source":"PubMed","id":"25533960","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues23
DetailsTransmembrane: {"description":"Helical; Name=7","evidences":[{"source":"PubMed","id":"25533960","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"25533960","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4S0V","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues1
DetailsSite: {"description":"Important for responses to orexin","evidences":[{"source":"PubMed","id":"26950369","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

243911

PDB entries from 2025-10-29

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