4CNO
Structure of the Salmonella typhi Type I dehydroquinase inhibited by a 3-dehydroquinic 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 |
C | 0003855 | molecular_function | 3-dehydroquinate dehydratase activity |
C | 0008652 | biological_process | amino acid biosynthetic process |
C | 0009073 | biological_process | aromatic amino acid family biosynthetic process |
C | 0009423 | biological_process | chorismate biosynthetic process |
C | 0016829 | molecular_function | lyase activity |
C | 0046279 | biological_process | 3,4-dihydroxybenzoate biosynthetic process |
D | 0003855 | molecular_function | 3-dehydroquinate dehydratase activity |
D | 0008652 | biological_process | amino acid biosynthetic process |
D | 0009073 | biological_process | aromatic amino acid family biosynthetic process |
D | 0009423 | biological_process | chorismate biosynthetic process |
D | 0016829 | molecular_function | lyase activity |
D | 0046279 | biological_process | 3,4-dihydroxybenzoate biosynthetic process |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE 9PY A 301 |
Chain | Residue |
A | SER21 |
A | GLU46 |
A | ARG48 |
A | MET203 |
A | ARG213 |
A | PHE225 |
A | GLN236 |
A | HOH2011 |
A | HOH2013 |
site_id | AC2 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE 9PY B 301 |
Chain | Residue |
B | SER21 |
B | MET23 |
B | GLU46 |
B | ARG48 |
B | HIS143 |
B | MET203 |
B | MET205 |
B | ARG213 |
B | PHE225 |
B | GLN236 |
B | HOH2013 |
B | HOH2047 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE 9PY C 301 |
Chain | Residue |
C | SER21 |
C | GLU46 |
C | ARG48 |
C | ARG213 |
C | PHE225 |
C | HOH2019 |
site_id | AC4 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE 9PY D 301 |
Chain | Residue |
D | SER21 |
D | GLU46 |
D | ARG48 |
D | LYS170 |
D | ARG213 |
D | PHE225 |
D | GLN236 |
D | HOH2017 |
D | HOH2018 |
D | HOH2065 |
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 | 4 |
Details | ACT_SITE: Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_00214, ECO:0000305|PubMed:24957267 |
Chain | Residue | Details |
A | HIS143 | |
B | HIS143 | |
C | HIS143 | |
D | HIS143 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
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 | |
C | LYS170 | |
D | LYS170 |
site_id | SWS_FT_FI3 |
Number of Residues | 8 |
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 | |
C | SER21 | |
C | SER232 | |
D | SER21 | |
D | SER232 |
site_id | SWS_FT_FI4 |
Number of Residues | 12 |
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 | |
D | GLU46 | |
D | ARG213 | |
D | GLN236 | |
A | ARG213 | |
A | GLN236 | |
B | GLU46 | |
B | ARG213 | |
B | GLN236 | |
C | GLU46 | |
C | ARG213 | |
C | GLN236 |
site_id | SWS_FT_FI5 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00214, ECO:0000269|PubMed:10360352 |
Chain | Residue | Details |
A | ARG82 | |
B | ARG82 | |
C | ARG82 | |
D | 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 |
site_id | MCSA3 |
Number of Residues | 3 |
Details | M-CSA 54 |
Chain | Residue | Details |
C | GLU86 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
C | HIS143 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
C | LYS170 | covalently attached, electron pair acceptor, electron pair donor, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor |
site_id | MCSA4 |
Number of Residues | 3 |
Details | M-CSA 54 |
Chain | Residue | Details |
D | GLU86 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
D | HIS143 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
D | LYS170 | covalently attached, electron pair acceptor, electron pair donor, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor |