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4BUO

High Resolution Structure of Thermostable Agonist-bound Neurotensin Receptor 1 Mutant without Lysozyme Fusion

Functional Information from GO Data
ChainGOidnamespacecontents
A0004930molecular_functionG protein-coupled receptor activity
A0007186biological_processG protein-coupled receptor signaling pathway
A0016020cellular_componentmembrane
A0016492molecular_functionG protein-coupled neurotensin receptor activity
B0004930molecular_functionG protein-coupled receptor activity
B0007186biological_processG protein-coupled receptor signaling pathway
B0016020cellular_componentmembrane
B0016492molecular_functionG protein-coupled neurotensin receptor activity
Functional Information from PDB Data
site_idAC1
Number of Residues1
DetailsBINDING SITE FOR RESIDUE GLY A 1385
ChainResidue
APHE206

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE GLY A 1386
ChainResidue
AASP103
ATYR104

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GLY A 1387
ChainResidue
AGLU166
AMET181
BPHE243

site_idAC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE GLY A 1389
ChainResidue
ALEU322
AVAL326

site_idAC5
Number of Residues1
DetailsBINDING SITE FOR RESIDUE GLY A 1390
ChainResidue
AALA140

site_idAC6
Number of Residues1
DetailsBINDING SITE FOR RESIDUE GLY A 1391
ChainResidue
APHE206

site_idAC7
Number of Residues1
DetailsBINDING SITE FOR RESIDUE GLY B 1387
ChainResidue
BTRP194

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GLY B 1388
ChainResidue
BGLN99
BARG305
BSER373
BASN375

site_idAC9
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GLY B 1389
ChainResidue
ALEU247
APHE248
BLEU180
BMET181
BPHE189

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues40
DetailsTransmembrane: {"description":"Helical; Name=1"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues38
DetailsTransmembrane: {"description":"Helical; Name=2"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues128
DetailsTopological domain: {"description":"Extracellular","evidences":[{"source":"PubMed","id":"24453215","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues42
DetailsTransmembrane: {"description":"Helical; Name=3"}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues38
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"24453215","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues40
DetailsTransmembrane: {"description":"Helical; Name=4"}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues48
DetailsTransmembrane: {"description":"Helical; Name=5"}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues42
DetailsTransmembrane: {"description":"Helical; Name=6"}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues40
DetailsTransmembrane: {"description":"Helical; Name=7"}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues46
DetailsRegion: {"description":"Neurotensin binding"}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues1
DetailsLipidation: {"description":"S-palmitoyl cysteine","evidences":[{"source":"UniProtKB","id":"P30989","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues2
DetailsSite: {"description":"Cleavage; by MME","evidences":[{"source":"UniProtKB","id":"P30990","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues2
DetailsSite: {"description":"Cleavage; by ACE and MME","evidences":[{"source":"UniProtKB","id":"P30990","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

246905

PDB entries from 2025-12-31

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