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2QQ2

Crystal structure of C-terminal domain of Human acyl-CoA thioesterase 7

Functional Information from GO Data
ChainGOidnamespacecontents
A0016790molecular_functionthiolester hydrolase activity
B0016790molecular_functionthiolester hydrolase activity
C0016790molecular_functionthiolester hydrolase activity
D0016790molecular_functionthiolester hydrolase activity
E0016790molecular_functionthiolester hydrolase activity
F0016790molecular_functionthiolester hydrolase activity
G0016790molecular_functionthiolester hydrolase activity
H0016790molecular_functionthiolester hydrolase activity
I0016790molecular_functionthiolester hydrolase activity
J0016790molecular_functionthiolester hydrolase activity
K0016790molecular_functionthiolester hydrolase activity
L0016790molecular_functionthiolester hydrolase activity
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues120
DetailsCompositional bias: {"description":"Basic and acidic residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues12
DetailsActive site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues12
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues456
DetailsDomain: {"description":"HotDog ACOT-type 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU01106","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

239803

PDB entries from 2025-08-06

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