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4XES

Structure of active-like neurotensin receptor

Functional Information from GO Data
ChainGOidnamespacecontents
A0003796molecular_functionlysozyme activity
A0004930molecular_functionG protein-coupled receptor activity
A0007186biological_processG protein-coupled receptor signaling pathway
A0009253biological_processpeptidoglycan catabolic process
A0016020cellular_componentmembrane
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
DetailsSITE: Cleavage; by MME => ECO:0000250|UniProtKB:P30990
ChainResidueDetails
BPRO10

site_idSWS_FT_FI2
Number of Residues1
DetailsSITE: Cleavage; by ACE and MME => ECO:0000250|UniProtKB:P30990
ChainResidueDetails
BTYR11
AALA166-ARG185
AALA261-LEU308

site_idSWS_FT_FI3
Number of Residues19
DetailsTRANSMEM: Helical; Name=2
ChainResidueDetails
ATYR104-VAL123

site_idSWS_FT_FI4
Number of Residues64
DetailsTOPO_DOM: Extracellular => ECO:0000269|PubMed:24453215
ChainResidueDetails
AGLU124-ARG143
ATHR207-LYS235
APHE331-HIS348

site_idSWS_FT_FI5
Number of Residues21
DetailsTRANSMEM: Helical; Name=3
ChainResidueDetails
AGLY144-VAL165

site_idSWS_FT_FI6
Number of Residues20
DetailsTRANSMEM: Helical; Name=4
ChainResidueDetails
ATHR186-PHE206

site_idSWS_FT_FI7
Number of Residues24
DetailsTRANSMEM: Helical; Name=5
ChainResidueDetails
AVAL236-ILE260

site_idSWS_FT_FI8
Number of Residues21
DetailsTRANSMEM: Helical; Name=6
ChainResidueDetails
AVAL309-MET330

site_idSWS_FT_FI9
Number of Residues20
DetailsTRANSMEM: Helical; Name=7
ChainResidueDetails
ATYR349-TYR369

site_idSWS_FT_FI10
Number of Residues2
DetailsLIPID: S-palmitoyl cysteine => ECO:0000250|UniProtKB:P30989
ChainResidueDetails
ACYS978
ACYS980

site_idSWS_FT_FI11
Number of Residues1
DetailsACT_SITE: Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_04110, ECO:0000269|PubMed:3382407, ECO:0000269|PubMed:7831309, ECO:0000269|PubMed:8266098
ChainResidueDetails
AGLU1011

site_idSWS_FT_FI12
Number of Residues1
DetailsACT_SITE: Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_04110, ECO:0000269|PubMed:1892846, ECO:0000269|PubMed:3382407, ECO:0000269|PubMed:7831309, ECO:0000269|PubMed:8266098
ChainResidueDetails
AASP1020

site_idSWS_FT_FI13
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:8266098
ChainResidueDetails
ALEU1032
APHE1104

site_idSWS_FT_FI14
Number of Residues2
DetailsBINDING: BINDING => ECO:0000303|PubMed:7831309
ChainResidueDetails
ASER1117
AASN1132

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 2024-10-30

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