2XDA
STRUCTURE OF HELICOBACTER PYLORI TYPE II DEHYDROQUINASE IN COMPLEX WITH INHIBITOR COMPOUND (4R,6R,7S)-2-(2-Cyclopropyl)ethyl-4,6,7- trihydroxy-4,5,6,7-tetrahydrobenzo(b)thiophene-4-carboxylic 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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE JPS A 1151 |
| Chain | Residue |
| A | ASN10 |
| A | LEU93 |
| A | HIS102 |
| A | LEU103 |
| A | THR104 |
| A | ARG113 |
| A | MET13 |
| A | ARG17 |
| A | TYR22 |
| A | ASN76 |
| A | GLY78 |
| A | ALA79 |
| A | HIS82 |
| A | ASP89 |
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 | 1 |
| Details | ACT_SITE: Proton acceptor |
| Chain | Residue | Details |
| A | TYR22 | |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | ACT_SITE: Proton donor |
| Chain | Residue | Details |
| A | HIS102 | |
| Chain | Residue | Details |
| A | ASN76 | |
| A | HIS82 | |
| A | ASP89 | |
| A | ARG113 | |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | LEU103 | |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | SITE: Transition state stabilizer |
| Chain | Residue | Details |
| A | ARG17 | |
