2XD9
STRUCTURE OF HELICOBACTER PYLORI TYPE II DEHYDROQUINASE IN COMPLEX WITH INHIBITOR COMPOUND (4R,6R,7S)-4,6,7-Trihydroxy-2-((E)-prop-1- enyl)-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 |
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 | 14 |
Details | BINDING SITE FOR RESIDUE XD9 A 200 |
Chain | Residue |
A | ASN10 |
A | LEU103 |
A | THR104 |
A | ARG113 |
A | HOH2003 |
B | ASP89 |
A | LEU11 |
A | LEU14 |
A | TYR22 |
A | ASN76 |
A | GLY78 |
A | ALA79 |
A | HIS82 |
A | HIS102 |
site_id | AC2 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE XD9 B 200 |
Chain | Residue |
B | ASN10 |
B | LEU14 |
B | TYR22 |
B | ASN76 |
B | GLY78 |
B | ALA79 |
B | HIS82 |
B | HIS102 |
B | LEU103 |
B | THR104 |
B | ARG113 |
B | HOH2099 |
C | ASP89 |
site_id | AC3 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE XD9 C 200 |
Chain | Residue |
A | ASP89 |
C | ASN10 |
C | LEU11 |
C | LEU14 |
C | TYR22 |
C | ASN76 |
C | GLY78 |
C | ALA79 |
C | HIS82 |
C | HIS102 |
C | LEU103 |
C | THR104 |
C | ARG113 |
C | HOH2089 |
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 | |
C | HIS82 | |
C | ASP89 | |
C | ARG113 | |
A | HIS82 | |
A | ASP89 | |
A | ARG113 | |
B | ASN76 | |
B | HIS82 | |
B | ASP89 | |
B | ARG113 | |
C | ASN76 |
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 |