8B2B
Crystal structure of type I dehydroquinase from Salmonella typhi inhibited by an epoxide derivative
This is a non-PDB format compatible entry.
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| AAA | 0003855 | molecular_function | 3-dehydroquinate dehydratase activity |
| AAA | 0008652 | biological_process | amino acid biosynthetic process |
| AAA | 0009073 | biological_process | aromatic amino acid family biosynthetic process |
| AAA | 0009423 | biological_process | chorismate biosynthetic process |
| AAA | 0016829 | molecular_function | lyase activity |
| AAA | 0046279 | biological_process | 3,4-dihydroxybenzoate biosynthetic process |
| BBB | 0003855 | molecular_function | 3-dehydroquinate dehydratase activity |
| BBB | 0008652 | biological_process | amino acid biosynthetic process |
| BBB | 0009073 | biological_process | aromatic amino acid family biosynthetic process |
| BBB | 0009423 | biological_process | chorismate biosynthetic process |
| BBB | 0016829 | molecular_function | lyase activity |
| BBB | 0046279 | biological_process | 3,4-dihydroxybenzoate biosynthetic process |
Functional Information from PROSITE/UniProt
| site_id | PS01028 |
| Number of Residues | 31 |
| Details | DEHYDROQUINASE_I Dehydroquinase class I active site. DLELftgdadvkatvdyahahnvyVVmSNHD |
| Chain | Residue | Details |
| AAA | ASP114-ASP144 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_00214, ECO:0000305|PubMed:24957267 |
| Chain | Residue | Details |
| AAA | HIS143 | |
| BBB | HIS143 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | ACT_SITE: Schiff-base intermediate with substrate => ECO:0000255|HAMAP-Rule:MF_00214, ECO:0000269|PubMed:10360352, ECO:0000269|PubMed:11976491 |
| Chain | Residue | Details |
| AAA | LYS170 | |
| BBB | LYS170 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00214, ECO:0000269|PubMed:10360352, ECO:0000269|PubMed:11976491 |
| Chain | Residue | Details |
| AAA | SER21 | |
| AAA | SER232 | |
| BBB | SER21 | |
| BBB | SER232 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00214, ECO:0000269|PubMed:10360352, ECO:0000269|PubMed:11976491, ECO:0000269|PubMed:24957267 |
| Chain | Residue | Details |
| AAA | GLU46 | |
| AAA | ARG213 | |
| AAA | GLN236 | |
| BBB | GLU46 | |
| BBB | ARG213 | |
| BBB | GLN236 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00214, ECO:0000269|PubMed:10360352 |
| Chain | Residue | Details |
| AAA | ARG82 | |
| BBB | ARG82 |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 3 |
| Details | M-CSA 54 |
| Chain | Residue | Details |
| AAA | GLU86 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| AAA | HIS143 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
| AAA | LYS170 | covalently attached, electron pair acceptor, electron pair donor, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor |
| site_id | MCSA2 |
| Number of Residues | 3 |
| Details | M-CSA 54 |
| Chain | Residue | Details |
| BBB | GLU86 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| BBB | HIS143 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
| BBB | LYS170 | covalently attached, electron pair acceptor, electron pair donor, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor |
