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4XEE

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 Residues4
Detailsbinding site for residue 1PE A 1201
ChainResidue
ATHR258
ALEU308
AARG311
AILE315

site_idAC2
Number of Residues2
Detailsbinding site for residue 1PE A 1202
ChainResidue
AHIS305
AARG377

site_idAC3
Number of Residues6
Detailsbinding site for residue EPE A 1203
ChainResidue
AGLN1105
AMET1106
AASP1159
AGLY1030
ALYS1035
APHE1104

site_idAC4
Number of Residues4
Detailsbinding site for residue FLC A 1204
ChainResidue
AASP56
AVAL57
ATRP130
AHIS132

site_idAC5
Number of Residues2
Detailsbinding site for residue PEG A 1205
ChainResidue
AARG1125
BARG8

Functional Information from PROSITE/UniProt
site_idPS00237
Number of Residues17
DetailsG_PROTEIN_RECEP_F1_1 G-protein coupled receptors family 1 signature. ATAlNVASLSVERYLaI
ChainResidueDetails
AALA155-ILE171

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
AGLU166-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

226707

PDB entries from 2024-10-30

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