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 | ACT_SITE: Proton acceptor |
Chain | Residue | Details |
A | TYR22 | |
B | TYR22 | |
C | TYR22 | |
D | TYR22 | |
E | TYR22 | |
F | TYR22 |
site_id | SWS_FT_FI2 |
Number of Residues | 6 |
Details | ACT_SITE: Proton donor |
Chain | Residue | Details |
A | HIS102 | |
B | HIS102 | |
C | HIS102 | |
D | HIS102 | |
E | HIS102 | |
F | HIS102 |
site_id | SWS_FT_FI3 |
Number of Residues | 24 |
Details | BINDING: BINDING => ECO:0000269|PubMed:12784220 |
Chain | Residue | Details |
A | ASN76 | |
C | HIS82 | |
C | ASP89 | |
C | ARG113 | |
D | ASN76 | |
D | HIS82 | |
D | ASP89 | |
D | ARG113 | |
E | ASN76 | |
E | HIS82 | |
E | ASP89 | |
A | HIS82 | |
E | ARG113 | |
F | ASN76 | |
F | HIS82 | |
F | ASP89 | |
F | ARG113 | |
A | ASP89 | |
A | ARG113 | |
B | ASN76 | |
B | HIS82 | |
B | ASP89 | |
B | ARG113 | |
C | ASN76 |
site_id | SWS_FT_FI4 |
Number of Residues | 6 |
Details | BINDING: |
Chain | Residue | Details |
A | LEU103 | |
B | LEU103 | |
C | LEU103 | |
D | LEU103 | |
E | LEU103 | |
F | LEU103 |
site_id | SWS_FT_FI5 |
Number of Residues | 6 |
Details | SITE: Transition state stabilizer |
Chain | Residue | Details |
A | ARG17 | |
B | ARG17 | |
C | ARG17 | |
D | ARG17 | |
E | ARG17 | |
F | ARG17 |
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 |