2VDJ
Crystal Structure of Homoserine O-acetyltransferase (metA) from Bacillus Cereus with Homoserine
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004414 | molecular_function | homoserine O-acetyltransferase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0008652 | biological_process | amino acid biosynthetic process |
| A | 0008899 | molecular_function | homoserine O-succinyltransferase activity |
| A | 0009086 | biological_process | methionine biosynthetic process |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016746 | molecular_function | acyltransferase activity |
| A | 0019281 | biological_process | L-methionine biosynthetic process from homoserine via O-succinyl-L-homoserine and cystathionine |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 A1297 |
| Chain | Residue |
| A | SER239 |
| A | CYS240 |
| A | ARG278 |
| A | HOH2164 |
| site_id | AC2 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE HSE A1298 |
| Chain | Residue |
| A | GLU246 |
| A | ARG249 |
| A | HOH2030 |
| A | HOH2165 |
| A | HOH2166 |
| A | CYS142 |
| A | LYS163 |
| A | SER192 |
| A | HIS235 |
| A | TYR238 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Acyl-thioester intermediate","evidences":[{"source":"HAMAP-Rule","id":"MF_00295","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"17546672","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"18216013","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_00295","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"17546672","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"18216013","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Active site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00295","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"17546672","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"18216013","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00295","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"18216013","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2VDJ","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Site: {"description":"Important for acyl-CoA specificity","evidences":[{"source":"HAMAP-Rule","id":"MF_00295","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | Site: {"description":"Important for substrate specificity","evidences":[{"source":"HAMAP-Rule","id":"MF_00295","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
