4CLM
Structure of Salmonella typhi type I dehydroquinase irreversibly inhibited with a 1,3,4-trihydroxyciclohexane-1-carboxylic 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 | 12 |
| Details | BINDING SITE FOR RESIDUE WPL B 301 |
| Chain | Residue |
| B | SER21 |
| B | ALA233 |
| B | GLN236 |
| B | HOH2129 |
| B | GLU46 |
| B | ARG48 |
| B | ARG82 |
| B | LYS170 |
| B | MET205 |
| B | ARG213 |
| B | PHE225 |
| B | SER232 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL A 1253 |
| Chain | Residue |
| A | HIS96 |
| A | THR99 |
| B | TYR130 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CL A 1254 |
| Chain | Residue |
| A | ARG159 |
| A | GLN162 |
| A | HOH2181 |
| A | HOH2310 |
| A | HOH2313 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CL A 1255 |
| Chain | Residue |
| A | LYS170 |
| A | LI1256 |
| A | HOH2358 |
| A | HOH2360 |
| A | HOH2393 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE LI A 1256 |
| Chain | Residue |
| A | ARG48 |
| A | ARG82 |
| A | LYS170 |
| A | CL1255 |
| A | HOH2078 |
| A | HOH2151 |
| A | HOH2210 |
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 | ACT_SITE: Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_00214, ECO:0000305|PubMed:24957267 |
| Chain | Residue | Details |
| A | HIS143 | |
| B | 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 |
| A | LYS170 | |
| B | 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 |
| A | SER21 | |
| A | SER232 | |
| B | SER21 | |
| B | 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 |
| A | GLU46 | |
| A | ARG213 | |
| A | GLN236 | |
| B | GLU46 | |
| B | ARG213 | |
| B | 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 |
| A | ARG82 | |
| B | ARG82 |
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 |
