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3GOA

Crystal structure of the Salmonella typhimurium FadA 3-ketoacyl-CoA thiolase

Functional Information from GO Data
ChainGOidnamespacecontents
A0003988molecular_functionacetyl-CoA C-acyltransferase activity
A0005737cellular_componentcytoplasm
A0006631biological_processfatty acid metabolic process
A0006635biological_processfatty acid beta-oxidation
A0010124biological_processphenylacetate catabolic process
A0016042biological_processlipid catabolic process
A0016746molecular_functionacyltransferase activity
A0016747molecular_functionacyltransferase activity, transferring groups other than amino-acyl groups
A0044281biological_processsmall molecule metabolic process
B0003988molecular_functionacetyl-CoA C-acyltransferase activity
B0005737cellular_componentcytoplasm
B0006631biological_processfatty acid metabolic process
B0006635biological_processfatty acid beta-oxidation
B0010124biological_processphenylacetate catabolic process
B0016042biological_processlipid catabolic process
B0016746molecular_functionacyltransferase activity
B0016747molecular_functionacyltransferase activity, transferring groups other than amino-acyl groups
B0044281biological_processsmall molecule metabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CA B 388
ChainResidue
BHOH419
BHOH694
BHOH756
BHOH773

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA B 389
ChainResidue
BHOH512
BHOH601
BHOH835
BHOH935
BHOH936

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CL A 388
ChainResidue
AALA9
AARG41
ATHR187
AGLU188
AARG264
AASN358

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL A 389
ChainResidue
AALA265
AARG266
AVAL387
AHOH934

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE NA B 390
ChainResidue
BARG266
BGLU385
BHOH939

Functional Information from PROSITE/UniProt
site_idPS00098
Number of Residues19
DetailsTHIOLASE_1 Thiolases acyl-enzyme intermediate signature. VNRlCGSSMqALhdaarmI
ChainResidueDetails
AVAL87-ILE105

site_idPS00099
Number of Residues14
DetailsTHIOLASE_3 Thiolases active site. GLATMCIGlGqGiA
ChainResidueDetails
AGLY368-ALA381

site_idPS00178
Number of Residues11
DetailsAA_TRNA_LIGASE_I Aminoacyl-transfer RNA synthetases class-I signature. Pv.SGtVTAGTS
ChainResidueDetails
APRO228-SER238

site_idPS00737
Number of Residues17
DetailsTHIOLASE_2 Thiolases signature 2. NlnGGaIAlGHPlGcSG
ChainResidueDetails
AASN333-GLY349

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Acyl-thioester intermediate => ECO:0000255|HAMAP-Rule:MF_01620
ChainResidueDetails
ACYS91
BCYS91

site_idSWS_FT_FI2
Number of Residues4
DetailsACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_01620
ChainResidueDetails
AHIS343
ACYS373
BHIS343
BCYS373

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1afw
ChainResidueDetails
AGLY375
AHIS343
ACYS91
ACYS373

site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 1afw
ChainResidueDetails
BGLY375
BHIS343
BCYS91
BCYS373

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1afw
ChainResidueDetails
AHIS343
ACYS373

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1afw
ChainResidueDetails
BHIS343
BCYS373

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PDB entries from 2024-07-24

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