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5WQC

Crystal structure of human orexin 2 receptor bound to the selective antagonist EMPA determined by the synchrotron light source at SPring-8.

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 Residues14
Detailsbinding site for residue 7MA A 2001
ChainResidue
APRO131
AVAL353
ATYR354
AHOH4022
AHOH4031
AHOH4092
AGLN187
AHIS224
APHE227
ATYR317
AILE320
ASER321
AASN324
AHIS350

site_idAC2
Number of Residues2
Detailsbinding site for residue OLA A 3001
ChainResidue
APHE366
AOLA3003

site_idAC3
Number of Residues3
Detailsbinding site for residue OLA A 3002
ChainResidue
ALEU150
ALEU229
AVAL230

site_idAC4
Number of Residues4
Detailsbinding site for residue OLA A 3003
ChainResidue
AILE315
ACYS316
AALA355
AOLA3001

site_idAC5
Number of Residues5
Detailsbinding site for residue OLA A 3004
ChainResidue
AGLU52
ATYR53
AVAL56
ALEU57
AGLY60

site_idAC6
Number of Residues4
Detailsbinding site for residue OLA A 3005
ChainResidue
ATYR219
AASN365
APHE366
AARG372

site_idAC7
Number of Residues3
Detailsbinding site for residue 1PE A 3501
ChainResidue
AASP211
ALYS327
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
DetailsTRANSMEM: Helical; Name=1 => ECO:0000269|PubMed:25533960
ChainResidueDetails
ATRP55-VAL75

site_idSWS_FT_FI2
Number of Residues31
DetailsTOPO_DOM: Cytoplasmic => ECO:0000269|PubMed:25533960
ChainResidueDetails
ACYS76-VAL88
AASP151-ARG170

site_idSWS_FT_FI3
Number of Residues21
DetailsTRANSMEM: Helical; Name=2 => ECO:0000269|PubMed:25533960
ChainResidueDetails
ATHR89-ALA110

site_idSWS_FT_FI4
Number of Residues61
DetailsTOPO_DOM: Extracellular => ECO:0000269|PubMed:25533960
ChainResidueDetails
ATHR111-CYS127
AGLU192-MET222
ALYS327-VAL342

site_idSWS_FT_FI5
Number of Residues22
DetailsTRANSMEM: Helical; Name=3 => ECO:0000269|PubMed:25533960
ChainResidueDetails
ALYS128-LEU150

site_idSWS_FT_FI6
Number of Residues20
DetailsTRANSMEM: Helical; Name=4 => ECO:0000269|PubMed:25533960
ChainResidueDetails
AASN171-MET191

site_idSWS_FT_FI7
Number of Residues20
DetailsTRANSMEM: Helical; Name=5 => ECO:0000269|PubMed:25533960
ChainResidueDetails
ATYR223-TYR243

site_idSWS_FT_FI8
Number of Residues21
DetailsTRANSMEM: Helical; Name=6 => ECO:0000269|PubMed:25533960
ChainResidueDetails
AMET305-LEU326

site_idSWS_FT_FI9
Number of Residues23
DetailsTRANSMEM: Helical; Name=7 => ECO:0000269|PubMed:25533960
ChainResidueDetails
ATYR343-PHE366

site_idSWS_FT_FI10
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:25533960, ECO:0007744|PDB:4S0V
ChainResidueDetails
AASN324

site_idSWS_FT_FI11
Number of Residues1
DetailsSITE: Important for responses to orexin => ECO:0000269|PubMed:26950369
ChainResidueDetails
ATRP44

site_idSWS_FT_FI12
Number of Residues3
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN14
AASN22
AASN202

219869

PDB entries from 2024-05-15

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