4V0S
Crystal structure of Mycobacterium tuberculosis Type II Dehydroquinase D88N mutant inhibited by a 3-dehydroquinic acid derivative
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003855 | molecular_function | 3-dehydroquinate dehydratase activity |
| A | 0005829 | cellular_component | cytosol |
| 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 | 0019631 | biological_process | quinate catabolic process |
| B | 0003855 | molecular_function | 3-dehydroquinate dehydratase activity |
| B | 0005829 | cellular_component | cytosol |
| 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 | 0019631 | biological_process | quinate catabolic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE 2HN A 1147 |
| Chain | Residue |
| A | PRO11 |
| A | GLY78 |
| A | HIS101 |
| A | ILE102 |
| A | SER103 |
| A | HOH2060 |
| A | ASN12 |
| A | LEU13 |
| A | ARG15 |
| A | LEU16 |
| A | ARG19 |
| A | TYR24 |
| A | ASN75 |
| A | GLY77 |
| site_id | AC2 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE 2HN A 1148 |
| Chain | Residue |
| A | ASN6 |
| A | ILE8 |
| A | VAL48 |
| A | ARG50 |
| A | TRP61 |
| A | GLN64 |
| A | ALA65 |
| A | HOH2048 |
| A | HOH2088 |
| A | HOH2089 |
| B | HIS29 |
| B | ASP30 |
| site_id | AC3 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE 7HN A 1149 |
| Chain | Residue |
| A | ASP60 |
| A | HIS63 |
| A | ASP67 |
| A | ARG87 |
| A | ASN88 |
| A | ALA91 |
| A | HOH2047 |
| A | HOH2065 |
| B | ALA34 |
| B | GLU37 |
| B | ARG38 |
| site_id | AC4 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE 2HN B 1145 |
| Chain | Residue |
| A | GLU42 |
| B | PRO11 |
| B | ASN12 |
| B | LEU13 |
| B | LEU16 |
| B | ARG19 |
| B | TYR24 |
| B | ASN75 |
| B | GLY77 |
| B | GLY78 |
| B | HIS101 |
| B | ILE102 |
| B | SER103 |
| B | ARG108 |
| B | HOH2046 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL A 1150 |
| Chain | Residue |
| A | GLN131 |
| A | ARG138 |
| site_id | AC6 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL B 1146 |
| Chain | Residue |
| B | GLN131 |
| B | ARG138 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE NA A 1151 |
| Chain | Residue |
| A | GLU39 |
| A | GLU42 |
| B | GLU20 |
| B | HOH2011 |
Functional Information from PROSITE/UniProt
| site_id | PS01029 |
| Number of Residues | 18 |
| Details | DEHYDROQUINASE_II Dehydroquinase class II signature. INGPNLgrLGrREpavYG |
| Chain | Residue | Details |
| A | ILE8-GLY25 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton acceptor |
| Chain | Residue | Details |
| A | TYR24 | |
| B | TYR24 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton donor |
| Chain | Residue | Details |
| A | HIS101 | |
| B | HIS101 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 10 |
| Details | BINDING: |
| Chain | Residue | Details |
| B | ILE102 | |
| B | ARG112 | |
| A | ASN75 | |
| A | HIS81 | |
| A | ASN88 | |
| A | ILE102 | |
| A | ARG112 | |
| B | ASN75 | |
| B | HIS81 | |
| B | ASN88 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | SITE: Transition state stabilizer |
| Chain | Residue | Details |
| A | ARG19 | |
| B | ARG19 |
