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3KUV

Structural basis of the activity and substrate specificity of the fluoroacetyl-CoA thioesterase FlK - T42S mutant in complex with 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 ACT A 140
ChainResidue
AALA41
ASER42
AACT141
AHOH213
AHOH214
BGLU50
BGLY69

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ACT A 141
ChainResidue
AACT140
AHOH213
BLEU68
BGLY69
AHIS76
AALA78

site_idAC3
Number of Residues11
DetailsBINDING SITE FOR RESIDUE ACT A 142
ChainResidue
AGLU50
AVAL54
AGLY69
AARG120
AHOH402
AHOH411
BVAL23
BPHE33
BPHE36
BACT142
BHOH362

site_idAC4
Number of Residues9
DetailsBINDING SITE FOR RESIDUE ACT B 140
ChainResidue
BALA71
BARG93
BSER94
BARG99
BARG99
BSER101
BGLU119
BGLU119
BHOH247

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE ACT B 141
ChainResidue
ASER42
AHIS76
BGLY69
BTHR70
BALA71
BILE72
BHIS118

site_idAC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE ACT B 142
ChainResidue
AGLY69
AACT142
AHOH411
BPHE40
BALA41
BSER42
BHOH362

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ACT B 143
ChainResidue
AALA71
AILE72
ACYS73
AHOH158
BVAL74
BARG103

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

246704

PDB entries from 2025-12-24

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