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3KVU

Structural basis of the activity and substrate specificity of the fluoroacetyl-CoA FlK - T42S mutant in complex with Acetyl-CoA

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
C0016289molecular_functionacyl-CoA hydrolase activity
C0016787molecular_functionhydrolase activity
C0042803molecular_functionprotein homodimerization activity
D0016289molecular_functionacyl-CoA hydrolase activity
D0016787molecular_functionhydrolase activity
D0042803molecular_functionprotein homodimerization activity
Functional Information from PDB Data
site_idAC1
Number of Residues10
DetailsBINDING SITE FOR RESIDUE ACO A 201
ChainResidue
AVAL23
BGLY69
AALA41
ASER42
AHIS76
ATHR77
AALA78
AALA79
AHOH414
BGLU50

site_idAC2
Number of Residues19
DetailsBINDING SITE FOR RESIDUE ACO B 200
ChainResidue
AGLU50
AGLY69
AALA121
AILE123
ALYS127
APHE128
ALYS131
BVAL23
BVAL39
BPHE40
BALA41
BSER42
BHIS76
BTHR77
BALA78
BALA79
BASP111
BHOH365
BHOH453

site_idAC3
Number of Residues11
DetailsBINDING SITE FOR RESIDUE ACO D 202
ChainResidue
CGLU50
CLEU68
CGLY69
CARG99
CALA121
DSER42
DHIS76
DTHR77
DALA78
DALA79
DHOH405

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues12
DetailsActive site: {}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues44
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"20430898","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20836570","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

238582

PDB entries from 2025-07-09

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