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 | 0003824 | molecular_function | catalytic activity |
| A | 0004315 | molecular_function | 3-oxoacyl-[acyl-carrier-protein] synthase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006629 | biological_process | lipid metabolic process |
| A | 0006631 | biological_process | fatty acid metabolic process |
| A | 0006633 | biological_process | fatty acid biosynthetic process |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016746 | molecular_function | acyltransferase activity |
| A | 0030497 | biological_process | fatty acid elongation |
| A | 0033818 | molecular_function | beta-ketoacyl-acyl-carrier-protein synthase III activity |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0004315 | molecular_function | 3-oxoacyl-[acyl-carrier-protein] synthase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0006629 | biological_process | lipid metabolic process |
| B | 0006631 | biological_process | fatty acid metabolic process |
| B | 0006633 | biological_process | fatty acid biosynthetic process |
| B | 0016740 | molecular_function | transferase activity |
| B | 0016746 | molecular_function | acyltransferase activity |
| B | 0030497 | biological_process | fatty acid elongation |
| B | 0033818 | molecular_function | beta-ketoacyl-acyl-carrier-protein synthase III activity |
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 | 8 |
| Details | Region: {"description":"ACP-binding","evidences":[{"source":"HAMAP-Rule","id":"MF_01815","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | Active site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01815","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10593943","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"10673437","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"11243824","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
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 |
