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5KW2

The extra-helical binding site of GPR40 and the structural basis for allosteric agonism and incretin stimulation

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 Residues15
Detailsbinding site for residue 6XQ A 2401
ChainResidue
APRO40
AILE130
ALEU189
ALEU193
APRO194
AILE197
AHOH2513
ATYR44
ATYR91
AGLY95
AALA99
AALA102
ATYR114
ASER123
AVAL126

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues63
DetailsTOPO_DOM: Extracellular => ECO:0000255, ECO:0000269|PubMed:25043059
ChainResidueDetails
AMET1-SER8
AGLU65-CYS79
AGLY143-SER178
ALEU2249-SER2256

site_idSWS_FT_FI2
Number of Residues22
DetailsTRANSMEM: Helical; Name=1 => ECO:0000255, ECO:0000269|PubMed:25043059
ChainResidueDetails
APHE9-THR31

site_idSWS_FT_FI3
Number of Residues48
DetailsTOPO_DOM: Cytoplasmic => ECO:0000255, ECO:0000269|PubMed:25043059
ChainResidueDetails
AALA32-SER41
AALA102-CYS121
AGLY2280-LYS2300

site_idSWS_FT_FI4
Number of Residues22
DetailsTRANSMEM: Helical; Name=2 => ECO:0000255, ECO:0000269|PubMed:25043059
ChainResidueDetails
AALA42-VAL64

site_idSWS_FT_FI5
Number of Residues21
DetailsTRANSMEM: Helical; Name=3 => ECO:0000255, ECO:0000269|PubMed:25043059
ChainResidueDetails
APRO80-SER101

site_idSWS_FT_FI6
Number of Residues20
DetailsTRANSMEM: Helical; Name=4 => ECO:0000255, ECO:0000269|PubMed:25043059
ChainResidueDetails
ATYR122-PHE142

site_idSWS_FT_FI7
Number of Residues21
DetailsTRANSMEM: Helical; Name=5 => ECO:0000255, ECO:0000269|PubMed:25043059
ChainResidueDetails
AALA179-PHE200

site_idSWS_FT_FI8
Number of Residues24
DetailsTRANSMEM: Helical; Name=6 => ECO:0000255, ECO:0000269|PubMed:25043059
ChainResidueDetails
ATRP2224-PHE2248

site_idSWS_FT_FI9
Number of Residues22
DetailsTRANSMEM: Helical; Name=7 => ECO:0000255, ECO:0000269|PubMed:25043059
ChainResidueDetails
ATRP2257-LEU2279

site_idSWS_FT_FI10
Number of Residues2
DetailsSITE: Important for receptor activation => ECO:0000269|PubMed:19068482
ChainResidueDetails
AGLU145
AGLU172

site_idSWS_FT_FI11
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN155

site_idSWS_FT_FI12
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_FI13
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_FI14
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:8266098
ChainResidueDetails
ALEU1032
APHE1104

site_idSWS_FT_FI15
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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