2WKS
Structure of Helicobacter pylori Type II Dehydroquinase with a new carbasugar-thiophene inhibitor.
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 |
| D | 0003855 | molecular_function | 3-dehydroquinate dehydratase activity |
| D | 0008652 | biological_process | amino acid biosynthetic process |
| D | 0009073 | biological_process | aromatic amino acid family biosynthetic process |
| D | 0009423 | biological_process | chorismate biosynthetic process |
| D | 0016829 | molecular_function | lyase activity |
| D | 0019631 | biological_process | quinate catabolic process |
| E | 0003855 | molecular_function | 3-dehydroquinate dehydratase activity |
| E | 0008652 | biological_process | amino acid biosynthetic process |
| E | 0009073 | biological_process | aromatic amino acid family biosynthetic process |
| E | 0009423 | biological_process | chorismate biosynthetic process |
| E | 0016829 | molecular_function | lyase activity |
| E | 0019631 | biological_process | quinate catabolic process |
| F | 0003855 | molecular_function | 3-dehydroquinate dehydratase activity |
| F | 0008652 | biological_process | amino acid biosynthetic process |
| F | 0009073 | biological_process | aromatic amino acid family biosynthetic process |
| F | 0009423 | biological_process | chorismate biosynthetic process |
| F | 0016829 | molecular_function | lyase activity |
| F | 0019631 | biological_process | quinate catabolic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE CB6 A 1154 |
| Chain | Residue |
| A | ASN10 |
| A | THR104 |
| A | ARG113 |
| B | ASP89 |
| B | LEU93 |
| A | LEU11 |
| A | TYR22 |
| A | ASN76 |
| A | GLY78 |
| A | ALA79 |
| A | HIS82 |
| A | HIS102 |
| A | LEU103 |
| site_id | AC2 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE CB6 B 1154 |
| Chain | Residue |
| B | LEU11 |
| B | LEU14 |
| B | TYR22 |
| B | ASN76 |
| B | GLY78 |
| B | ALA79 |
| B | HIS82 |
| B | HIS102 |
| B | LEU103 |
| B | THR104 |
| B | ARG113 |
| E | ASP89 |
| E | LEU93 |
| site_id | AC3 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE CB6 C 1154 |
| Chain | Residue |
| C | ASN10 |
| C | TYR22 |
| C | ASN76 |
| C | GLY78 |
| C | ALA79 |
| C | HIS82 |
| C | HIS102 |
| C | LEU103 |
| C | THR104 |
| C | ARG113 |
| F | ASP89 |
| F | LEU93 |
| site_id | AC4 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE CB6 D 1154 |
| Chain | Residue |
| C | ASP89 |
| C | LEU93 |
| D | ASN10 |
| D | LEU11 |
| D | TYR22 |
| D | ASN76 |
| D | GLY78 |
| D | ALA79 |
| D | HIS82 |
| D | HIS102 |
| D | LEU103 |
| D | THR104 |
| D | ARG113 |
| site_id | AC5 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE CB6 E 1154 |
| Chain | Residue |
| A | ASP89 |
| A | LEU93 |
| E | ASN10 |
| E | TYR22 |
| E | ASN76 |
| E | GLY78 |
| E | ALA79 |
| E | HIS82 |
| E | HIS102 |
| E | LEU103 |
| E | THR104 |
| E | ARG113 |
| site_id | AC6 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE CB6 F 1154 |
| Chain | Residue |
| D | ASP89 |
| D | LEU93 |
| F | ASN10 |
| F | TYR22 |
| F | ASN76 |
| F | GLY78 |
| F | ALA79 |
| F | HIS82 |
| F | HIS102 |
| F | LEU103 |
| F | THR104 |
| F | ARG113 |
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 | 6 |
| Details | Active site: {"description":"Proton acceptor"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | Active site: {"description":"Proton donor"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 24 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"12784220","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 6 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 6 |
| Details | Site: {"description":"Transition state stabilizer"} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 6 |
| Details | Annotated By Reference To The Literature 1uqr |
| Chain | Residue | Details |
| A | ARG109 | |
| A | HIS102 | |
| A | TYR22 | |
| A | ASN10 | |
| A | GLU100 | |
| A | ARG17 |
| site_id | CSA2 |
| Number of Residues | 6 |
| Details | Annotated By Reference To The Literature 1uqr |
| Chain | Residue | Details |
| B | ARG109 | |
| B | HIS102 | |
| B | TYR22 | |
| B | ASN10 | |
| B | GLU100 | |
| B | ARG17 |
| site_id | CSA3 |
| Number of Residues | 6 |
| Details | Annotated By Reference To The Literature 1uqr |
| Chain | Residue | Details |
| C | ARG109 | |
| C | HIS102 | |
| C | TYR22 | |
| C | ASN10 | |
| C | GLU100 | |
| C | ARG17 |
| site_id | CSA4 |
| Number of Residues | 6 |
| Details | Annotated By Reference To The Literature 1uqr |
| Chain | Residue | Details |
| D | ARG109 | |
| D | HIS102 | |
| D | TYR22 | |
| D | ASN10 | |
| D | GLU100 | |
| D | ARG17 |
| site_id | CSA5 |
| Number of Residues | 6 |
| Details | Annotated By Reference To The Literature 1uqr |
| Chain | Residue | Details |
| E | ARG109 | |
| E | HIS102 | |
| E | TYR22 | |
| E | ASN10 | |
| E | GLU100 | |
| E | ARG17 |
| site_id | CSA6 |
| Number of Residues | 6 |
| Details | Annotated By Reference To The Literature 1uqr |
| Chain | Residue | Details |
| F | ARG109 | |
| F | HIS102 | |
| F | TYR22 | |
| F | ASN10 | |
| F | GLU100 | |
| F | ARG17 |
