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 | 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 |