Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

4DJH

Structure of the human kappa opioid receptor in complex with JDTic

Functional Information from GO Data
ChainGOidnamespacecontents
A0003796molecular_functionlysozyme activity
A0003824molecular_functioncatalytic activity
A0004930molecular_functionG protein-coupled receptor activity
A0007186biological_processG protein-coupled receptor signaling pathway
A0009253biological_processpeptidoglycan catabolic process
A0016020cellular_componentmembrane
A0016787molecular_functionhydrolase activity
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0016998biological_processcell wall macromolecule catabolic process
A0030430cellular_componenthost cell cytoplasm
A0031640biological_processkilling of cells of another organism
A0042742biological_processdefense response to bacterium
A0044659biological_processviral release from host cell by cytolysis
B0003796molecular_functionlysozyme activity
B0003824molecular_functioncatalytic activity
B0004930molecular_functionG protein-coupled receptor activity
B0007186biological_processG protein-coupled receptor signaling pathway
B0009253biological_processpeptidoglycan catabolic process
B0016020cellular_componentmembrane
B0016787molecular_functionhydrolase activity
B0016798molecular_functionhydrolase activity, acting on glycosyl bonds
B0016998biological_processcell wall macromolecule catabolic process
B0030430cellular_componenthost cell cytoplasm
B0031640biological_processkilling of cells of another organism
B0042742biological_processdefense response to bacterium
B0044659biological_processviral release from host cell by cytolysis
Functional Information from PDB Data
site_idAC1
Number of Residues14
DetailsBINDING SITE FOR RESIDUE JDC A 1300
ChainResidue
ATHR111
AILE294
AILE316
ATYR320
AHOH1303
AHOH1304
AGLN115
AVAL134
AASP138
ATYR139
ALYS227
AVAL230
ATRP287
AILE290

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CIT A 1301
ChainResidue
AGLY1012
AARG1014
ATYR1018
AHOH1308

site_idAC3
Number of Residues16
DetailsBINDING SITE FOR RESIDUE JDC B 1300
ChainResidue
BTHR111
BGLN115
BLEU135
BASP138
BMET142
BCYS210
BLYS227
BVAL230
BTRP287
BILE294
BILE316
BTYR320
BHOH1307
BHOH1313
BHOH1314
BHOH1316

site_idAC4
Number of Residues9
DetailsBINDING SITE FOR RESIDUE OLC B 1302
ChainResidue
ATRP221
BTYR97
BASP155
BILE158
BPHE169
BLYS174
BILE178
BCYS181
BOLC1303

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE OLC B 1303
ChainResidue
AGLY300
ASER301
BTYR157
BHIS162
BPRO163
BVAL164
BOLC1302

site_idAC6
Number of Residues1
DetailsBINDING SITE FOR RESIDUE PEG B 1304
ChainResidue
BLEU299

site_idAC7
Number of Residues7
DetailsBINDING SITE FOR RESIDUE PEG B 1305
ChainResidue
APRO1037
ASER1038
ALEU1039
BTHR92
BTHR94
BARG270
BILE272

Functional Information from PROSITE/UniProt
site_idPS00237
Number of Residues17
DetailsG_PROTEIN_RECEP_F1_1 G-protein coupled receptors family 1 signature. TSIfTLTMMSVDRYIaV
ChainResidueDetails
ATHR144-VAL160

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
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 Residues2
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 Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"8266098","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"7831309","evidenceCode":"ECO:0000303"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues54
DetailsTransmembrane: {"description":"Helical; Name=1"}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues54
DetailsTopological domain: {"description":"Cytoplasmic"}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues46
DetailsTransmembrane: {"description":"Helical; Name=2"}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues74
DetailsTopological domain: {"description":"Extracellular"}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues42
DetailsTransmembrane: {"description":"Helical; Name=3"}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues44
DetailsTransmembrane: {"description":"Helical; Name=4"}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues48
DetailsTransmembrane: {"description":"Helical; Name=5"}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues42
DetailsTransmembrane: {"description":"Helical; Name=6"}
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues42
DetailsTransmembrane: {"description":"Helical; Name=7"}
ChainResidueDetails

site_idSWS_FT_FI14
Number of Residues2
DetailsLipidation: {"description":"S-palmitoyl cysteine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idMCSA1
Number of Residues2
DetailsM-CSA 921
ChainResidueDetails
AGLU1011proton shuttle (general acid/base)
AASP1020covalent catalysis

site_idMCSA2
Number of Residues2
DetailsM-CSA 921
ChainResidueDetails
BGLU1011proton shuttle (general acid/base)
BASP1020covalent catalysis

239492

PDB entries from 2025-07-30

PDB statisticsPDBj update infoContact PDBjnumon