1EBL
THE 1.8 A CRYSTAL STRUCTURE AND ACTIVE SITE ARCHITECTURE OF BETA-KETOACYL-[ACYL CARRIER PROTEIN] SYNTHASE III (FABH) FROM ESCHERICHIA COLI
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004315 | molecular_function | 3-oxoacyl-[acyl-carrier-protein] synthase activity |
A | 0005737 | cellular_component | cytoplasm |
A | 0005829 | cellular_component | cytosol |
A | 0006631 | biological_process | fatty acid metabolic process |
A | 0006633 | biological_process | fatty acid biosynthetic process |
A | 0016746 | molecular_function | acyltransferase activity |
A | 0033818 | molecular_function | beta-ketoacyl-acyl-carrier-protein synthase III activity |
A | 0044281 | biological_process | small molecule metabolic process |
B | 0004315 | molecular_function | 3-oxoacyl-[acyl-carrier-protein] synthase activity |
B | 0005737 | cellular_component | cytoplasm |
B | 0005829 | cellular_component | cytosol |
B | 0006631 | biological_process | fatty acid metabolic process |
B | 0006633 | biological_process | fatty acid biosynthetic process |
B | 0016746 | molecular_function | acyltransferase activity |
B | 0033818 | molecular_function | beta-ketoacyl-acyl-carrier-protein synthase III activity |
B | 0044281 | biological_process | small molecule metabolic process |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 26 |
Details | BINDING SITE FOR RESIDUE COA A 1350 |
Chain | Residue |
A | TRP32 |
A | PRO199 |
A | GLU200 |
A | MSE207 |
A | PHE213 |
A | HIS244 |
A | ASN247 |
A | ILE250 |
A | ASN274 |
A | HOH1445 |
A | HOH1503 |
A | ARG36 |
A | HOH1515 |
A | HOH1522 |
A | HOH1548 |
A | HOH1566 |
A | HOH1633 |
A | HOH1675 |
B | ARG144 |
A | THR37 |
A | CYS112 |
A | ARG151 |
A | GLY152 |
A | ILE156 |
A | ARG196 |
A | VAL197 |
site_id | AC2 |
Number of Residues | 28 |
Details | BINDING SITE FOR RESIDUE COA B 2350 |
Chain | Residue |
A | ASP225 |
A | GLU226 |
A | ALA229 |
A | HOH1565 |
A | HOH1579 |
A | HOH1646 |
A | HOH1663 |
A | HOH1678 |
B | ASP27 |
B | THR28 |
B | TRP32 |
B | THR37 |
B | CYS112 |
B | ARG151 |
B | GLY152 |
B | ILE155 |
B | ILE156 |
B | MSE207 |
B | GLY209 |
B | VAL212 |
B | PHE213 |
B | HIS244 |
B | ALA246 |
B | ASN247 |
B | ARG249 |
B | ASN274 |
B | HOH2472 |
B | HOH2620 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 6 |
Details | ACT_SITE: ACT_SITE => ECO:0000255|HAMAP-Rule:MF_01815, ECO:0000305|PubMed:10593943, ECO:0000305|PubMed:10673437, ECO:0000305|PubMed:11243824 |
Chain | Residue | Details |
A | CYS112 | |
A | HIS244 | |
A | ASN274 | |
B | CYS112 | |
B | HIS244 | |
B | ASN274 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1cgk |
Chain | Residue | Details |
A | ASN274 | |
A | CYS112 | |
A | PHE157 | |
A | HIS244 |
site_id | CSA2 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1cgk |
Chain | Residue | Details |
B | ASN274 | |
B | CYS112 | |
B | PHE157 | |
B | HIS244 |