1NUA
Crystal structure of 3-dehydroquinate synthase (DHQS) in complex with ZN2+
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003856 | molecular_function | 3-dehydroquinate synthase activity |
A | 0005737 | cellular_component | cytoplasm |
A | 0009073 | biological_process | aromatic amino acid family biosynthetic process |
A | 0016838 | molecular_function | carbon-oxygen lyase activity, acting on phosphates |
B | 0003856 | molecular_function | 3-dehydroquinate synthase activity |
B | 0005737 | cellular_component | cytoplasm |
B | 0009073 | biological_process | aromatic amino acid family biosynthetic process |
B | 0016838 | molecular_function | carbon-oxygen lyase activity, acting on phosphates |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN A 600 |
Chain | Residue |
A | ASP146 |
A | GLU194 |
A | HIS271 |
A | HIS287 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN B 601 |
Chain | Residue |
B | GLU194 |
B | HIS271 |
B | HIS287 |
B | HOH647 |
site_id | AC3 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CL B 602 |
Chain | Residue |
B | HOH614 |
B | HOH626 |
B | LYS89 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | ACT_SITE: Proton acceptor; for 3-dehydroquinate synthase activity |
Chain | Residue | Details |
A | GLU260 | |
A | HIS275 | |
B | GLU260 | |
B | HIS275 |
site_id | SWS_FT_FI2 |
Number of Residues | 22 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_03143, ECO:0000269|PubMed:12614613, ECO:0000269|PubMed:9685163 |
Chain | Residue | Details |
A | ASP44 | |
A | HIS271 | |
A | HIS287 | |
B | ASP44 | |
B | GLU81 | |
B | GLY114 | |
B | ASP119 | |
B | THR139 | |
B | LYS161 | |
B | PHE179 | |
B | ASN190 | |
A | GLU81 | |
B | GLU194 | |
B | HIS271 | |
B | HIS287 | |
A | GLY114 | |
A | ASP119 | |
A | THR139 | |
A | LYS161 | |
A | PHE179 | |
A | ASN190 | |
A | GLU194 |
site_id | SWS_FT_FI3 |
Number of Residues | 14 |
Details | BINDING: |
Chain | Residue | Details |
A | ARG130 | |
B | LYS152 | |
B | ASN162 | |
B | LYS250 | |
B | ARG264 | |
B | LYS356 | |
A | ASP146 | |
A | LYS152 | |
A | ASN162 | |
A | LYS250 | |
A | ARG264 | |
A | LYS356 | |
B | ARG130 | |
B | ASP146 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1dqs |
Chain | Residue | Details |
A | HIS275 |
site_id | CSA2 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1dqs |
Chain | Residue | Details |
B | HIS275 |
site_id | MCSA1 |
Number of Residues | 10 |
Details | M-CSA 59 |
Chain | Residue | Details |
A | ARG130 | electrostatic stabiliser |
A | HIS287 | metal ligand |
A | LYS152 | hydrogen bond donor, steric role |
A | GLU194 | metal ligand |
A | LYS250 | electrostatic stabiliser, hydrogen bond donor, steric role |
A | GLU260 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
A | ARG264 | electrostatic stabiliser, hydrogen bond donor, steric role |
A | ASN268 | hydrogen bond donor, steric role |
A | HIS271 | metal ligand |
A | HIS275 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
site_id | MCSA2 |
Number of Residues | 10 |
Details | M-CSA 59 |
Chain | Residue | Details |
B | ARG130 | electrostatic stabiliser |
B | HIS287 | metal ligand |
B | LYS152 | hydrogen bond donor, steric role |
B | GLU194 | metal ligand |
B | LYS250 | electrostatic stabiliser, hydrogen bond donor, steric role |
B | GLU260 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
B | ARG264 | electrostatic stabiliser, hydrogen bond donor, steric role |
B | ASN268 | hydrogen bond donor, steric role |
B | HIS271 | metal ligand |
B | HIS275 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |