4B6S
Structure of Helicobacter pylori Type II Dehydroquinase inhibited by (2S)-2-Perfluorobenzyl-3-dehydroquinic acid
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 | 0019631 | biological_process | quinate catabolic 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 | 0019631 | biological_process | quinate catabolic process |
| C | 0003855 | molecular_function | 3-dehydroquinate dehydratase activity |
| C | 0008652 | biological_process | amino acid biosynthetic process |
| C | 0009073 | biological_process | aromatic amino acid family biosynthetic process |
| C | 0009423 | biological_process | chorismate biosynthetic process |
| C | 0016829 | molecular_function | lyase activity |
| C | 0019631 | biological_process | quinate catabolic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE 2HN A 200 |
| Chain | Residue |
| A | ASN10 |
| A | LEU103 |
| A | THR104 |
| A | ARG113 |
| A | HOH2005 |
| C | ASP89 |
| C | LEU93 |
| C | HOH2033 |
| A | LEU11 |
| A | LEU14 |
| A | TYR22 |
| A | ASN76 |
| A | GLY78 |
| A | ALA79 |
| A | HIS82 |
| A | HIS102 |
| site_id | AC2 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE 2HN B 200 |
| Chain | Residue |
| A | ASP89 |
| A | LEU93 |
| A | HOH2063 |
| A | HOH2066 |
| B | PRO9 |
| B | ASN10 |
| B | LEU11 |
| B | LEU14 |
| B | TYR22 |
| B | ASN76 |
| B | GLY78 |
| B | ALA79 |
| B | HIS82 |
| B | HIS102 |
| B | LEU103 |
| B | THR104 |
| B | ARG113 |
| site_id | AC3 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE 2HN C 200 |
| Chain | Residue |
| B | ASP89 |
| B | LEU93 |
| B | HOH2045 |
| B | HOH2046 |
| B | HOH2047 |
| C | PRO9 |
| C | ASN10 |
| C | LEU11 |
| C | LEU14 |
| C | TYR22 |
| C | ASN76 |
| C | GLY78 |
| C | ALA79 |
| C | HIS82 |
| C | HIS102 |
| C | LEU103 |
| C | THR104 |
| C | ARG113 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PO4 A 1159 |
| Chain | Residue |
| A | PHE54 |
| A | GLU57 |
| B | PHE54 |
| B | GLU57 |
| C | GLU57 |
Functional Information from PROSITE/UniProt
| site_id | PS01029 |
| Number of Residues | 18 |
| Details | DEHYDROQUINASE_II Dehydroquinase class II signature. IQGPNLnmLGhRDprlYG |
| Chain | Residue | Details |
| A | ILE6-GLY23 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 3 |
| Details | ACT_SITE: Proton acceptor |
| Chain | Residue | Details |
| A | TYR22 | |
| B | TYR22 | |
| C | TYR22 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 3 |
| Details | ACT_SITE: Proton donor |
| Chain | Residue | Details |
| A | HIS102 | |
| B | HIS102 | |
| C | HIS102 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:12784220 |
| Chain | Residue | Details |
| A | ASN76 | |
| A | HIS82 | |
| A | ASP89 | |
| A | ARG113 | |
| B | ASN76 | |
| B | HIS82 | |
| B | ASP89 | |
| B | ARG113 | |
| C | ASN76 | |
| C | HIS82 | |
| C | ASP89 | |
| C | ARG113 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 3 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | LEU103 | |
| B | LEU103 | |
| C | LEU103 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 3 |
| Details | SITE: Transition state stabilizer |
| Chain | Residue | Details |
| A | ARG17 | |
| B | ARG17 | |
| C | ARG17 |
