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6W25

Crystal structure of the Melanocortin-4 Receptor (MC4R) in complex with SHU9119

Functional Information from GO Data
ChainGOidnamespacecontents
A0004930molecular_functionG protein-coupled receptor activity
A0004977molecular_functionmelanocortin receptor activity
A0007186biological_processG protein-coupled receptor signaling pathway
A0016020cellular_componentmembrane
Functional Information from PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue CA A 2101
ChainResidue
AGLU100
AASP122
AASP126
BASP2
B4J24

site_idAC2
Number of Residues2
Detailsbinding site for residue OLA A 2102
ChainResidue
AILE245
AARG305

site_idAC3
Number of Residues3
Detailsbinding site for residue OLA A 2103
ChainResidue
AOLA2104
AHIS214
APHE1124

site_idAC4
Number of Residues4
Detailsbinding site for residue OLA A 2104
ChainResidue
APRO1123
AASP1148
AOLA2103
AOLA2105

site_idAC5
Number of Residues8
Detailsbinding site for residue OLA A 2105
ChainResidue
AALA144
APHE152
AHIS222
AGLY1125
ALEU1129
AILE1149
APHE1195
AOLA2104

site_idAC6
Number of Residues2
Detailsbinding site for residue OLA A 2106
ChainResidue
ATYR212
APHE216

site_idAC7
Number of Residues2
Detailsbinding site for residue OLA A 2107
ChainResidue
APHE81
ATRP174

site_idAC8
Number of Residues1
Detailsbinding site for residue OLA A 2108
ChainResidue
AALA192

site_idAC9
Number of Residues1
Detailsbinding site for residue OLA A 2109
ChainResidue
AASP1148

site_idAD1
Number of Residues2
Detailsbinding site for residues ACE B 1 and NLE B 2
ChainResidue
AASP122
BASP2

Functional Information from PROSITE/UniProt
site_idPS00237
Number of Residues17
DetailsG_PROTEIN_RECEP_F1_1 G-protein coupled receptors family 1 signature. ASIcSLLSIAVDRYFtI
ChainResidueDetails
AALA135-ILE151

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues25
DetailsTransmembrane: {"description":"Helical; Name=1","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues30
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues24
DetailsTransmembrane: {"description":"Helical; Name=2","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues21
DetailsTransmembrane: {"description":"Helical; Name=3","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=4","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues12
DetailsTopological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues23
DetailsTransmembrane: {"description":"Helical; Name=5","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues22
DetailsTransmembrane: {"description":"Helical; Name=6","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues23
DetailsTransmembrane: {"description":"Helical; Name=7","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"32327598","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues1
DetailsLipidation: {"description":"S-palmitoyl cysteine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

246704

PDB entries from 2025-12-24

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