1QFE
THE STRUCTURE OF TYPE I 3-DEHYDROQUINATE DEHYDRATASE FROM SALMONELLA TYPHI
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 | 0046279 | biological_process | 3,4-dihydroxybenzoate biosynthetic 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 | 0046279 | biological_process | 3,4-dihydroxybenzoate biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE DHS A 301 |
| Chain | Residue |
| A | MET203 |
| A | ARG213 |
| A | PHE225 |
| A | SER232 |
| A | ALA233 |
| A | GLN236 |
| A | HOH409 |
| A | HOH461 |
| A | SER21 |
| A | GLU46 |
| A | ARG48 |
| A | ARG82 |
| A | HIS143 |
| A | LYS170 |
| site_id | AC2 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE DHS B 301 |
| Chain | Residue |
| B | SER21 |
| B | GLU46 |
| B | ARG48 |
| B | ARG82 |
| B | HIS143 |
| B | LYS170 |
| B | MET203 |
| B | ARG213 |
| B | PHE225 |
| B | SER232 |
| B | ALA233 |
| B | GLN236 |
| B | HOH410 |
| B | HOH452 |
| site_id | ASR |
| Number of Residues | 3 |
| Details | LYS 170 FORMS THE IMINE INTERMEDIATE WITH THE AID OF HIS 143 ARG 213 INTERACTS WITH THE CARBOXYL GROUP OF THE 3-DEHYDROQUINATE SUBSTRATE. |
| Chain | Residue |
| A | LYS170 |
| A | HIS143 |
| A | ARG213 |
Functional Information from PROSITE/UniProt
| site_id | PS01028 |
| Number of Residues | 31 |
| Details | DEHYDROQUINASE_I Dehydroquinase class I active site. DLELftgdadvkatvdyahahnvyVVmSNHD |
| Chain | Residue | Details |
| A | ASP114-ASP144 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_00214","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"24957267","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Schiff-base intermediate with substrate","evidences":[{"source":"HAMAP-Rule","id":"MF_00214","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10360352","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11976491","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00214","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10360352","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11976491","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00214","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10360352","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11976491","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24957267","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00214","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10360352","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | a catalytic site defined by CSA, PubMed 9545291, 10360352 |
| Chain | Residue | Details |
| A | LYS170 | |
| A | HIS143 | |
| A | GLU86 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | a catalytic site defined by CSA, PubMed 9545291, 10360352 |
| Chain | Residue | Details |
| B | LYS170 | |
| B | HIS143 | |
| B | GLU86 |
| site_id | MCSA1 |
| Number of Residues | 3 |
| Details | M-CSA 54 |
| Chain | Residue | Details |
| A | GLU86 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| A | HIS143 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
| A | 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 |
| B | GLU86 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| B | HIS143 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
| B | LYS170 | covalently attached, electron pair acceptor, electron pair donor, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor |
