5YDB
Crystal structure of the complex of type II dehydroquinate dehydratase from Acinetobacter baumannii with dehydroquinic acid at 1.76 Angstrom resolution
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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 2 |
| Details | binding site for residue NA A 201 |
| Chain | Residue |
| A | HIS107 |
| A | CYS127 |
| site_id | AC2 |
| Number of Residues | 10 |
| Details | binding site for residue DQA A 202 |
| Chain | Residue |
| A | SER104 |
| A | ARG113 |
| A | HOH310 |
| A | ASN76 |
| A | ALA78 |
| A | ALA79 |
| A | HIS82 |
| A | ASP89 |
| A | HIS102 |
| A | LEU103 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | binding site for residue NA B 201 |
| Chain | Residue |
| B | HIS107 |
| B | CYS127 |
| site_id | AC4 |
| Number of Residues | 10 |
| Details | binding site for residue DQA B 202 |
| Chain | Residue |
| B | ASN76 |
| B | ALA78 |
| B | ALA79 |
| B | HIS82 |
| B | HIS102 |
| B | LEU103 |
| B | SER104 |
| B | ARG113 |
| B | HOH324 |
| D | ASP89 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | binding site for residue NA C 201 |
| Chain | Residue |
| C | HIS107 |
| C | CYS127 |
| site_id | AC6 |
| Number of Residues | 11 |
| Details | binding site for residue DQA C 202 |
| Chain | Residue |
| B | ASP89 |
| C | ASN76 |
| C | ALA78 |
| C | ALA79 |
| C | HIS82 |
| C | HIS102 |
| C | LEU103 |
| C | SER104 |
| C | VAL106 |
| C | ARG113 |
| C | HOH309 |
| site_id | AC7 |
| Number of Residues | 2 |
| Details | binding site for residue NA D 201 |
| Chain | Residue |
| D | HIS107 |
| D | CYS127 |
| site_id | AC8 |
| Number of Residues | 11 |
| Details | binding site for residue DQA D 202 |
| Chain | Residue |
| C | ASP89 |
| D | ASN76 |
| D | ALA78 |
| D | ALA79 |
| D | HIS82 |
| D | HIS102 |
| D | LEU103 |
| D | SER104 |
| D | ARG109 |
| D | ARG113 |
| D | HOH313 |
Functional Information from PROSITE/UniProt
| site_id | PS01029 |
| Number of Residues | 18 |
| Details | DEHYDROQUINASE_II Dehydroquinase class II signature. IHGPNLnlLGkREpevYG |
| Chain | Residue | Details |
| A | ILE8-GLY25 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_00169","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"HAMAP-Rule","id":"MF_00169","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 20 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00169","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | Site: {"description":"Transition state stabilizer","evidences":[{"source":"HAMAP-Rule","id":"MF_00169","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
