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 | ACT_SITE: Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_00214 |
Chain | Residue | Details |
A | HIS133 | |
B | HIS133 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | ACT_SITE: Schiff-base intermediate with substrate => ECO:0000255|HAMAP-Rule:MF_00214 |
Chain | Residue | Details |
A | LYS160 | |
B | LYS160 |
site_id | SWS_FT_FI3 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00214 |
Chain | Residue | Details |
A | GLU35 | |
A | ARG70 | |
A | ARG202 | |
A | GLN225 | |
B | GLU35 | |
B | ARG70 | |
B | ARG202 | |
B | GLN225 |