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5ZBQ

The Crystal Structure of human neuropeptide Y Y1 receptor with UR-MK299

Functional Information from GO Data
ChainGOidnamespacecontents
A0001601molecular_functionpeptide YY receptor activity
A0001602molecular_functionpancreatic polypeptide receptor activity
A0003151biological_processoutflow tract morphogenesis
A0003796molecular_functionlysozyme activity
A0003824molecular_functioncatalytic activity
A0004930molecular_functionG protein-coupled receptor activity
A0004983molecular_functionneuropeptide Y receptor activity
A0005515molecular_functionprotein binding
A0005886cellular_componentplasma membrane
A0007154biological_processcell communication
A0007165biological_processsignal transduction
A0007186biological_processG protein-coupled receptor signaling pathway
A0007187biological_processG protein-coupled receptor signaling pathway, coupled to cyclic nucleotide second messenger
A0007193biological_processadenylate cyclase-inhibiting G protein-coupled receptor signaling pathway
A0007218biological_processneuropeptide signaling pathway
A0008188molecular_functionneuropeptide receptor activity
A0009253biological_processpeptidoglycan catabolic process
A0016020cellular_componentmembrane
A0016787molecular_functionhydrolase activity
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0016998biological_processcell wall macromolecule catabolic process
A0023052biological_processsignaling
A0030430cellular_componenthost cell cytoplasm
A0031640biological_processkilling of cells of another organism
A0042742biological_processdefense response to bacterium
A0043005cellular_componentneuron projection
A0044659biological_processviral release from host cell by cytolysis
A1904000biological_processpositive regulation of eating behavior
Functional Information from PDB Data
site_idAC1
Number of Residues13
Detailsbinding site for residue 9AO A 1301
ChainResidue
APRO117
AASN283
APHE286
AASP287
APHE302
AGLN120
ACYS121
AILE124
APHE173
ATHR212
AGLN219
ATHR280
APHE282

Functional Information from PROSITE/UniProt
site_idPS00237
Number of Residues17
DetailsG_PROTEIN_RECEP_F1_1 G-protein coupled receptors family 1 signature. VSIwSLVLIAVERHQlI
ChainResidueDetails
AVAL126-ILE142

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"description":"Proton donor/acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_04110","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"3382407","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7831309","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8266098","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsActive site: {"description":"Proton donor/acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_04110","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"1892846","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"3382407","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7831309","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8266098","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"8266098","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"7831309","evidenceCode":"ECO:0000303"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=1","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues26
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=2","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues70
DetailsTopological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=3","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=4","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=5","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=6","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=7","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idMCSA1
Number of Residues2
DetailsM-CSA 921
ChainResidueDetails
AGLU1010proton shuttle (general acid/base)
AASP1019covalent catalysis

250359

PDB entries from 2026-03-11

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