8B2A
Crystal structure of type I dehydroquinase from Staphylococcus aureus inhibited by a hydroxylamine derivative
This is a non-PDB format compatible entry.
Functional Information from GO Data
Chain | GOid | namespace | contents |
AAA | 0003855 | molecular_function | 3-dehydroquinate dehydratase activity |
AAA | 0008652 | biological_process | amino acid biosynthetic process |
AAA | 0009073 | biological_process | aromatic amino acid family biosynthetic process |
AAA | 0009423 | biological_process | chorismate biosynthetic process |
AAA | 0016829 | molecular_function | lyase activity |
AAA | 0046279 | biological_process | 3,4-dihydroxybenzoate biosynthetic process |
BBB | 0003855 | molecular_function | 3-dehydroquinate dehydratase activity |
BBB | 0008652 | biological_process | amino acid biosynthetic process |
BBB | 0009073 | biological_process | aromatic amino acid family biosynthetic process |
BBB | 0009423 | biological_process | chorismate biosynthetic process |
BBB | 0016829 | molecular_function | lyase activity |
BBB | 0046279 | biological_process | 3,4-dihydroxybenzoate biosynthetic process |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_00214","evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | Active site: {"description":"Schiff-base intermediate with substrate","evidences":[{"source":"HAMAP-Rule","id":"MF_00214","evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 10 |
Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00214","evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |