2GHR
Crystal structure of homoserine o-succinyltransferase (NP_981826.1) from Bacillus cereus ATCC 10987 at 2.40 A resolution
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 | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 A 302 |
| Chain | Residue |
| A | SER239 |
| A | CYS240 |
| A | ARG278 |
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 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1qdl |
| Chain | Residue | Details |
| A | CYS142 | |
| A | GLU237 | |
| A | HIS235 |
