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3P2R

Crystal structure of the fluoroacetyl-CoA-specific thioesterase FlK in complex with fluoroacetate

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
ALEU68
AGLY69
AFAH143
BPHE40
BTHR42
BFAH140

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FAH A 141
ChainResidue
AALA79
AFAH142
BGLY69
AHIS76
AALA78

site_idAC3
Number of Residues10
DetailsBINDING SITE FOR RESIDUE FAH A 142
ChainResidue
AVAL23
APHE36
AALA41
ATHR42
AFAH141
AFAH144
BGLU50
BLEU68
BGLY69
BFAH141

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE FAH A 143
ChainResidue
AGLU50
AARG120
AFAH140
BVAL23
BPHE33
BPHE36

site_idAC5
Number of Residues10
DetailsBINDING SITE FOR RESIDUE FAH A 144
ChainResidue
AVAL23
ALEU26
APHE33
AALA41
ATHR42
AGLY43
AFAH142
BGLY47
BGLU50
BFAH141

site_idAC6
Number of Residues8
DetailsBINDING SITE FOR RESIDUE FAH B 140
ChainResidue
ALEU68
AGLY69
ATHR70
AFAH140
BHIS76
BTHR77
BALA78
BALA79

site_idAC7
Number of Residues8
DetailsBINDING SITE FOR RESIDUE FAH B 141
ChainResidue
APHE33
APHE36
AFAH142
AFAH144
BGLU50
BSER67
BGLY69
BARG120

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsActive site: {}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues22
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"20430898","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20836570","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

249524

PDB entries from 2026-02-18

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