6SFH
CRYSTAL STRUCTURE OF DHQ1 FROM Staphylococcus aureus COVALENTLY MODIFIED BY LIGAND 7
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003855 | molecular_function | 3-dehydroquinate dehydratase activity |
| A | 0008652 | biological_process | amino acid biosynthetic process |
| A | 0009073 | biological_process | aromatic amino acid family biosynthetic process |
| A | 0009423 | biological_process | chorismate biosynthetic process |
| A | 0016829 | molecular_function | lyase activity |
| A | 0046279 | biological_process | 3,4-dihydroxybenzoate biosynthetic process |
| B | 0003855 | molecular_function | 3-dehydroquinate dehydratase activity |
| B | 0008652 | biological_process | amino acid biosynthetic process |
| B | 0009073 | biological_process | aromatic amino acid family biosynthetic process |
| B | 0009423 | biological_process | chorismate biosynthetic process |
| B | 0016829 | molecular_function | lyase activity |
| B | 0046279 | biological_process | 3,4-dihydroxybenzoate biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 14 |
| Details | binding site for residue L9Z A 301 |
| Chain | Residue |
| A | THR9 |
| A | TYR214 |
| A | ALA222 |
| A | GLN225 |
| A | HOH464 |
| A | HOH514 |
| A | GLU35 |
| A | ARG37 |
| A | THR68 |
| A | ARG70 |
| A | HIS133 |
| A | LYS160 |
| A | ILE192 |
| A | ARG202 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue SO4 A 302 |
| Chain | Residue |
| A | TYR15 |
| A | GLU17 |
| A | GLU18 |
| A | LYS55 |
| A | HOH483 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue LI A 303 |
| Chain | Residue |
| A | GLN234 |
| A | TYR238 |
| B | GLN234 |
| B | TYR238 |
| site_id | AC4 |
| Number of Residues | 20 |
| Details | binding site for Di-peptide L9Z B 301 and LYS B 160 |
| Chain | Residue |
| B | THR9 |
| B | GLU35 |
| B | ARG37 |
| B | THR68 |
| B | ARG70 |
| B | ILE130 |
| B | SER131 |
| B | HIS132 |
| B | HIS133 |
| B | MET151 |
| B | VAL159 |
| B | LEU161 |
| B | VAL190 |
| B | ILE192 |
| B | ARG202 |
| B | TYR214 |
| B | ALA222 |
| B | GLN225 |
| B | HOH443 |
| B | HOH457 |
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 |
