4CNP
Structure of the Salmonella typhi type I dehydroquinase inhibited by a 3-epiquinic acid derivative
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 | 15 |
| Details | BINDING SITE FOR RESIDUE 9C4 A 301 |
| Chain | Residue |
| A | SER21 |
| A | SER232 |
| A | ALA233 |
| A | GLN236 |
| A | HOH2150 |
| A | HOH2202 |
| A | HOH2355 |
| A | GLU46 |
| A | ARG48 |
| A | ARG82 |
| A | LYS170 |
| A | ALA172 |
| A | MET203 |
| A | ARG213 |
| A | PHE225 |
| site_id | AC2 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE 9C4 B 301 |
| Chain | Residue |
| B | SER21 |
| B | GLU46 |
| B | ARG48 |
| B | ARG82 |
| B | LYS170 |
| B | ALA172 |
| B | MET203 |
| B | ARG213 |
| B | PHE225 |
| B | SER232 |
| B | ALA233 |
| B | GLN236 |
| B | HOH2095 |
| B | HOH2133 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE NA A 1253 |
| Chain | Residue |
| A | GLU33 |
| A | HOH2077 |
| A | HOH2111 |
| A | HOH2393 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA A 1254 |
| Chain | Residue |
| A | ASN135 |
| A | HOH2241 |
| A | HOH2243 |
| A | HOH2271 |
| A | HOH2273 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA B 1253 |
| Chain | Residue |
| A | ALA56 |
| A | HIS96 |
| B | TYR130 |
| B | HIS134 |
| B | HOH2274 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA A 1255 |
| Chain | Residue |
| A | TYR130 |
| A | HIS134 |
| A | HOH2264 |
| A | HOH2394 |
| B | ALA56 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE NA B 1254 |
| Chain | Residue |
| B | SER83 |
| B | ALA84 |
| B | GLN90 |
| B | THR91 |
| B | ILE92 |
| B | HOH2135 |
| B | HOH2149 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE NA A 1256 |
| Chain | Residue |
| A | PHE81 |
| A | ASN101 |
| A | ASP114 |
| site_id | AC9 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE NA B 1255 |
| Chain | Residue |
| B | PHE81 |
| B | ASN101 |
| B | ASP114 |
| site_id | BC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL B 1256 |
| Chain | Residue |
| A | HIS96 |
| A | THR99 |
| B | ARG102 |
| B | TYR130 |
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 | 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 |
