4CKZ
Structure of the Mycobacterium tuberculosis Type II Dehydroquinase D88N mutant
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003855 | molecular_function | 3-dehydroquinate dehydratase activity |
A | 0005829 | cellular_component | cytosol |
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 | 0005829 | cellular_component | cytosol |
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 |
Functional Information from PROSITE/UniProt
site_id | PS01029 |
Number of Residues | 18 |
Details | DEHYDROQUINASE_II Dehydroquinase class II signature. INGPNLgrLGrREpavYG |
Chain | Residue | Details |
A | ILE8-GLY25 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Proton acceptor |
Chain | Residue | Details |
A | TYR24 | |
B | TYR24 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | ACT_SITE: Proton donor |
Chain | Residue | Details |
A | HIS101 | |
B | HIS101 |
site_id | SWS_FT_FI3 |
Number of Residues | 10 |
Details | BINDING: |
Chain | Residue | Details |
B | ILE102 | |
B | ARG112 | |
B | HIS81 | |
B | ASN88 | |
A | ASN75 | |
A | HIS81 | |
A | ASN88 | |
A | ILE102 | |
A | ARG112 | |
B | ASN75 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | SITE: Transition state stabilizer |
Chain | Residue | Details |
A | ARG19 | |
B | ARG19 |