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3KVZ

Structural basis of the activity and substrate specificity of the fluoroacetyl-CoA thiesterase FlK - wild type FlK in complex with FAcCPan

Functional Information from GO Data
ChainGOidnamespacecontents
A0016289molecular_functionacyl-CoA hydrolase activity
A0042803molecular_functionprotein homodimerization activity
B0016289molecular_functionacyl-CoA hydrolase activity
B0042803molecular_functionprotein homodimerization activity
C0016289molecular_functionacyl-CoA hydrolase activity
C0042803molecular_functionprotein homodimerization activity
D0016289molecular_functionacyl-CoA hydrolase activity
D0042803molecular_functionprotein homodimerization activity
E0016289molecular_functionacyl-CoA hydrolase activity
E0042803molecular_functionprotein homodimerization activity
F0016289molecular_functionacyl-CoA hydrolase activity
F0042803molecular_functionprotein homodimerization activity
G0016289molecular_functionacyl-CoA hydrolase activity
G0042803molecular_functionprotein homodimerization activity
H0016289molecular_functionacyl-CoA hydrolase activity
H0042803molecular_functionprotein homodimerization activity
Functional Information from PDB Data
site_idAC1
Number of Residues12
DetailsBINDING SITE FOR RESIDUE ENV B 201
ChainResidue
AGLU50
BGLY43
BHIS76
BALA79
ALEU68
AGLY69
AHOH166
BVAL23
BLEU26
BVAL39
BALA41
BTHR42

site_idAC2
Number of Residues12
DetailsBINDING SITE FOR RESIDUE ENV E 202
ChainResidue
EGLU50
ELEU68
EGLY69
EHOH348
EHOH689
FVAL23
FLEU26
FPHE33
FVAL39
FALA41
FTHR42
FGLY43

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues24
DetailsActive site: {}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues88
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues16
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"20430898","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20836570","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

251174

PDB entries from 2026-03-25

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