Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

5VEX

Structure of the human GLP-1 receptor complex with NNC0640

Functional Information from GO Data
ChainGOidnamespacecontents
A0003796molecular_functionlysozyme activity
A0003824molecular_functioncatalytic activity
A0004888molecular_functiontransmembrane signaling receptor activity
A0004930molecular_functionG protein-coupled receptor activity
A0007166biological_processcell surface receptor signaling pathway
A0007186biological_processG protein-coupled receptor signaling pathway
A0008152biological_processmetabolic process
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
B0004888molecular_functiontransmembrane signaling receptor activity
B0004930molecular_functionG protein-coupled receptor activity
B0007166biological_processcell surface receptor signaling pathway
B0007186biological_processG protein-coupled receptor signaling pathway
B0008152biological_processmetabolic process
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 Residues9
Detailsbinding site for residue 97V A 1201
ChainResidue
APHE347
AARG348
ALYS351
ASER352
ALEU354
ATHR355
ALEU401
AVAL405
AASN406

site_idAC2
Number of Residues8
Detailsbinding site for residue 97V B 1201
ChainResidue
BPHE347
BARG348
BLYS351
BSER352
BTHR355
BLEU401
BVAL405
BASN406

Functional Information from PROSITE/UniProt
site_idPS00650
Number of Residues16
DetailsG_PROTEIN_RECEP_F2_2 G-protein coupled receptors family 2 signature 2. QGLMVaILYCFvNneV
ChainResidueDetails
AGLN394-VAL409

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues48
DetailsTRANSMEM: Helical; Name=1 => ECO:0000269|PubMed:28514449
ChainResidueDetails
AGLN140-ALA164
BGLN140-ALA164

site_idSWS_FT_FI2
Number of Residues58
DetailsTOPO_DOM: Cytoplasmic => ECO:0000269|PubMed:28514449
ChainResidueDetails
AILE165-THR175
ACYS329-ARG348
BILE165-THR175
BCYS329-ARG348

site_idSWS_FT_FI3
Number of Residues50
DetailsTRANSMEM: Helical; Name=2 => ECO:0000269|PubMed:28514449
ChainResidueDetails
AARG176-LEU201
BARG176-LEU201

site_idSWS_FT_FI4
Number of Residues102
DetailsTOPO_DOM: Extracellular => ECO:0000269|PubMed:28514449
ChainResidueDetails
ALYS202-GLN234
ATYR291-TYR305
AMET371-LYS383
BLYS202-GLN234
BTYR291-TYR305
BMET371-LYS383

site_idSWS_FT_FI5
Number of Residues46
DetailsTRANSMEM: Helical; Name=3 => ECO:0000269|PubMed:28514449
ChainResidueDetails
ALEU228-LEU251
BLEU228-LEU251

site_idSWS_FT_FI6
Number of Residues48
DetailsTRANSMEM: Helical; Name=4 => ECO:0000269|PubMed:28514449
ChainResidueDetails
APHE266-LEU290
BPHE266-LEU290

site_idSWS_FT_FI7
Number of Residues44
DetailsTRANSMEM: Helical; Name=5 => ECO:0000269|PubMed:28514449
ChainResidueDetails
ATRP306-ILE328
BTRP306-ILE328

site_idSWS_FT_FI8
Number of Residues42
DetailsTRANSMEM: Helical; Name=6 => ECO:0000269|PubMed:28514449
ChainResidueDetails
ALEU349-VAL370
BLEU349-VAL370

site_idSWS_FT_FI9
Number of Residues40
DetailsTRANSMEM: Helical; Name=7 => ECO:0000269|PubMed:28514449
ChainResidueDetails
ALEU384-PHE404
BLEU384-PHE404

site_idSWS_FT_FI10
Number of Residues2
DetailsSITE: Interaction with the endogenous ligand GLP-1 => ECO:0000269|PubMed:19861722
ChainResidueDetails
AGLU128
BGLU128

site_idSWS_FT_FI11
Number of Residues2
DetailsMOD_RES: ADP-ribosylcysteine => ECO:0000269|PubMed:21901419
ChainResidueDetails
ACYS341
BCYS341

site_idSWS_FT_FI12
Number of Residues2
DetailsMOD_RES: ADP-ribosylarginine => ECO:0000269|PubMed:21901419
ChainResidueDetails
AARG348
BARG348

site_idSWS_FT_FI13
Number of Residues2
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
BGLU1011

site_idSWS_FT_FI14
Number of Residues2
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
BASP1020

site_idSWS_FT_FI15
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:8266098
ChainResidueDetails
ALEU1032
APHE1104
BLEU1032
BPHE1104

site_idSWS_FT_FI16
Number of Residues4
DetailsBINDING: BINDING => ECO:0000303|PubMed:7831309
ChainResidueDetails
ASER1117
AASN1132
BSER1117
BASN1132

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

218853

PDB entries from 2024-04-24

PDB statisticsPDBj update infoContact PDBjnumon