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4XES

Structure of active-like neurotensin receptor

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
Functional Information from PDB Data
site_idAC1
Number of Residues10
Detailsbinding site for residue CIT A 1201
ChainResidue
AARG299
ASER1165
AARG1008
AILE1009
APHE1114
ATHR1115
AASN1116
ASER1117
AASN1132
ASER1163

site_idAC2
Number of Residues4
Detailsbinding site for residue PEG A 1202
ChainResidue
ACYS172
ALYS263
ALEU1079
APEG1203

site_idAC3
Number of Residues6
Detailsbinding site for residue PEG A 1203
ChainResidue
ALYS263
AMET267
AVAL1075
ATYR1088
AARG1096
APEG1202

site_idAC4
Number of Residues3
Detailsbinding site for residue PEG A 1204
ChainResidue
ALEU303
APHE1004
AASN1068

site_idAC5
Number of Residues8
Detailsbinding site for residue PEG A 1206
ChainResidue
AARG1080
AASN1081
AALA1082
AGLU1108
ATHR1109
ATYR1139
APRO1143
AASN1144

site_idAC6
Number of Residues2
Detailsbinding site for residue GOL A 1207
ChainResidue
AARG1125
BARG8

site_idAC7
Number of Residues1
Detailsbinding site for residue GOL A 1208
ChainResidue
ATYR349

site_idAC8
Number of Residues5
Detailsbinding site for residue GOL A 1209
ChainResidue
ALYS1083
ATHR1142
APRO1143
AASN1144
AARG1145

site_idAC9
Number of Residues8
Detailsbinding site for residue EPE A 1210
ChainResidue
AGLY1030
AHIS1031
ALEU1032
ALYS1035
AASP1070
APHE1104
AMET1106
AASP1159

site_idAD1
Number of Residues5
Detailsbinding site for residue EPE A 1211
ChainResidue
AASP56
AVAL57
ATRP130
AHIS132
AHIS133

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"}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues32
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"24453215","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues19
DetailsTransmembrane: {"description":"Helical; Name=2"}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues64
DetailsTopological domain: {"description":"Extracellular","evidences":[{"source":"PubMed","id":"24453215","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues21
DetailsTransmembrane: {"description":"Helical; Name=3"}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=4"}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues24
DetailsTransmembrane: {"description":"Helical; Name=5"}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues21
DetailsTransmembrane: {"description":"Helical; Name=6"}
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=7"}
ChainResidueDetails

site_idSWS_FT_FI14
Number of Residues23
DetailsRegion: {"description":"Neurotensin binding"}
ChainResidueDetails

site_idSWS_FT_FI15
Number of Residues1
DetailsSite: {"description":"Cleavage; by MME","evidences":[{"source":"UniProtKB","id":"P30990","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI16
Number of Residues1
DetailsSite: {"description":"Cleavage; by ACE and MME","evidences":[{"source":"UniProtKB","id":"P30990","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

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

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PDB entries from 2025-12-17

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