3GOA
Crystal structure of the Salmonella typhimurium FadA 3-ketoacyl-CoA thiolase
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003988 | molecular_function | acetyl-CoA C-acyltransferase activity |
A | 0005737 | cellular_component | cytoplasm |
A | 0006631 | biological_process | fatty acid metabolic process |
A | 0006635 | biological_process | fatty acid beta-oxidation |
A | 0010124 | biological_process | phenylacetate catabolic process |
A | 0016042 | biological_process | lipid catabolic process |
A | 0016746 | molecular_function | acyltransferase activity |
A | 0016747 | molecular_function | acyltransferase activity, transferring groups other than amino-acyl groups |
A | 0044281 | biological_process | small molecule metabolic process |
B | 0003988 | molecular_function | acetyl-CoA C-acyltransferase activity |
B | 0005737 | cellular_component | cytoplasm |
B | 0006631 | biological_process | fatty acid metabolic process |
B | 0006635 | biological_process | fatty acid beta-oxidation |
B | 0010124 | biological_process | phenylacetate catabolic process |
B | 0016042 | biological_process | lipid catabolic process |
B | 0016746 | molecular_function | acyltransferase activity |
B | 0016747 | molecular_function | acyltransferase activity, transferring groups other than amino-acyl groups |
B | 0044281 | biological_process | small molecule metabolic process |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CA B 388 |
Chain | Residue |
B | HOH419 |
B | HOH694 |
B | HOH756 |
B | HOH773 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CA B 389 |
Chain | Residue |
B | HOH512 |
B | HOH601 |
B | HOH835 |
B | HOH935 |
B | HOH936 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CL A 388 |
Chain | Residue |
A | ALA9 |
A | ARG41 |
A | THR187 |
A | GLU188 |
A | ARG264 |
A | ASN358 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CL A 389 |
Chain | Residue |
A | ALA265 |
A | ARG266 |
A | VAL387 |
A | HOH934 |
site_id | AC5 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE NA B 390 |
Chain | Residue |
B | ARG266 |
B | GLU385 |
B | HOH939 |
Functional Information from PROSITE/UniProt
site_id | PS00098 |
Number of Residues | 19 |
Details | THIOLASE_1 Thiolases acyl-enzyme intermediate signature. VNRlCGSSMqALhdaarmI |
Chain | Residue | Details |
A | VAL87-ILE105 |
site_id | PS00099 |
Number of Residues | 14 |
Details | THIOLASE_3 Thiolases active site. GLATMCIGlGqGiA |
Chain | Residue | Details |
A | GLY368-ALA381 |
site_id | PS00178 |
Number of Residues | 11 |
Details | AA_TRNA_LIGASE_I Aminoacyl-transfer RNA synthetases class-I signature. Pv.SGtVTAGTS |
Chain | Residue | Details |
A | PRO228-SER238 |
site_id | PS00737 |
Number of Residues | 17 |
Details | THIOLASE_2 Thiolases signature 2. NlnGGaIAlGHPlGcSG |
Chain | Residue | Details |
A | ASN333-GLY349 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Acyl-thioester intermediate => ECO:0000255|HAMAP-Rule:MF_01620 |
Chain | Residue | Details |
A | CYS91 | |
B | CYS91 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | ACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_01620 |
Chain | Residue | Details |
A | HIS343 | |
A | CYS373 | |
B | HIS343 | |
B | CYS373 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1afw |
Chain | Residue | Details |
A | GLY375 | |
A | HIS343 | |
A | CYS91 | |
A | CYS373 |
site_id | CSA2 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1afw |
Chain | Residue | Details |
B | GLY375 | |
B | HIS343 | |
B | CYS91 | |
B | CYS373 |
site_id | CSA3 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1afw |
Chain | Residue | Details |
A | HIS343 | |
A | CYS373 |
site_id | CSA4 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1afw |
Chain | Residue | Details |
B | HIS343 | |
B | CYS373 |