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3KUW

Structural basis of the activity ans substrate specificity of the fluoroacetyl-CoA thioesterase FlK - T42S mutant in complex with Fluoro-acetate

Functional Information from GO Data
ChainGOidnamespacecontents
A0016289molecular_functionacyl-CoA hydrolase activity
A0016787molecular_functionhydrolase activity
A0042803molecular_functionprotein homodimerization activity
B0016289molecular_functionacyl-CoA hydrolase activity
B0016787molecular_functionhydrolase activity
B0042803molecular_functionprotein homodimerization activity
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE FAH A 140
ChainResidue
AGLU50
AARG120
AHOH426
BPHE36
BALA41
BSER42
BHOH365

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE FAH A 141
ChainResidue
ASER42
AFAH142
AHOH430
BGLU50
BLEU68
BGLY69
APHE36
AALA41

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE FAH A 142
ChainResidue
AHIS76
AALA78
AALA79
AFAH141
AHOH184
BGLY69

site_idAC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE FAH B 140
ChainResidue
ASER42
AHIS76
BGLU50
BGLY69
BTHR70
BALA71
BILE72
BHIS118

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsACT_SITE:
ChainResidueDetails
ASER42
AGLU50
AHIS76
BSER42
BGLU50
BHIS76

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING:
ChainResidueDetails
BPHE40
BHIS76
APHE40
AHIS76

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:20430898, ECO:0000269|PubMed:20836570
ChainResidueDetails
BGLY69
BARG120
AGLY69
AARG120

219869

PDB entries from 2024-05-15

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