1FHU
CRYSTAL STRUCTURE ANALYSIS OF O-SUCCINYLBENZOATE SYNTHASE FROM E. COLI
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0009234 | biological_process | menaquinone biosynthetic process |
| A | 0016829 | molecular_function | lyase activity |
| A | 0016836 | molecular_function | hydro-lyase activity |
| A | 0043748 | molecular_function | O-succinylbenzoate synthase activity |
| A | 0046872 | molecular_function | metal ion binding |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"HAMAP-Rule","id":"MF_00470","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10978150","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_00470","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10978150","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00470","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10978150","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1r6w |
| Chain | Residue | Details |
| A | LYS133 | |
| A | LYS235 |
| site_id | MCSA1 |
| Number of Residues | 5 |
| Details | M-CSA 689 |
| Chain | Residue | Details |
| A | LYS133 | proton acceptor, proton donor |
| A | ASP161 | metal ligand |
| A | GLU190 | metal ligand |
| A | ASP213 | metal ligand |
| A | LYS235 | electrostatic stabiliser |
