1NRX
Crystal structure of 3-dehydroquinate synthase (DHQS) in complex with ZN2+ and NAD
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 | 3 |
Details | BINDING SITE FOR RESIDUE ZN B 1601 |
Chain | Residue |
B | GLU194 |
B | HIS271 |
B | HIS287 |
site_id | AC3 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE CL B 607 |
Chain | Residue |
B | ARG12 |
site_id | AC4 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE CL A 608 |
Chain | Residue |
A | ARG12 |
site_id | AC5 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CL A 609 |
Chain | Residue |
A | ALA279 |
A | GLN347 |
A | ASN351 |
site_id | AC6 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CL A 613 |
Chain | Residue |
A | ARG130 |
A | HOH723 |
B | LYS152 |
site_id | AC7 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE CL B 619 |
Chain | Residue |
B | LEU72 |
site_id | AC8 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE CL B 623 |
Chain | Residue |
B | LYS309 |
site_id | AC9 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE CL B 625 |
Chain | Residue |
B | GLN347 |
site_id | BC1 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE CL A 626 |
Chain | Residue |
A | GLN99 |
site_id | BC2 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE CL B 627 |
Chain | Residue |
B | THR282 |
B | LYS341 |
site_id | BC3 |
Number of Residues | 20 |
Details | BINDING SITE FOR RESIDUE NAD A 400 |
Chain | Residue |
A | ASP44 |
A | ASN46 |
A | GLU81 |
A | LYS84 |
A | GLY114 |
A | GLY115 |
A | VAL116 |
A | ASP119 |
A | THR139 |
A | THR140 |
A | ASP146 |
A | SER147 |
A | LYS152 |
A | ASN162 |
A | PHE179 |
A | THR182 |
A | LEU183 |
A | GLU187 |
A | HOH635 |
A | HOH637 |
site_id | BC4 |
Number of Residues | 21 |
Details | BINDING SITE FOR RESIDUE NAD B 401 |
Chain | Residue |
B | ASP44 |
B | ASN46 |
B | ILE47 |
B | GLU81 |
B | LYS84 |
B | GLY114 |
B | GLY115 |
B | VAL116 |
B | ASP119 |
B | THR139 |
B | THR140 |
B | ASP146 |
B | SER147 |
B | LYS152 |
B | ASN162 |
B | PHE179 |
B | THR182 |
B | LEU183 |
B | PRO184 |
B | GLU187 |
B | HOH1703 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | Active site: {"description":"Proton acceptor; for 3-dehydroquinate synthase activity"} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 34 |
Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_03143","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"12614613","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9685163","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 24 |
Details | Binding site: {} |
Chain | Residue | Details |
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 | 9 |
Details | M-CSA 59 |
Chain | Residue | Details |
A | ARG130 | electrostatic stabiliser |
A | LYS152 | hydrogen bond donor, steric role |
A | GLU194 | metal ligand |
A | LYS250 | electrostatic stabiliser, hydrogen bond donor, steric role |
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 |
A | HIS287 | metal ligand |
site_id | MCSA2 |
Number of Residues | 9 |
Details | M-CSA 59 |
Chain | Residue | Details |
B | ARG130 | electrostatic stabiliser |
B | LYS152 | hydrogen bond donor, steric role |
B | GLU194 | metal ligand |
B | LYS250 | electrostatic stabiliser, hydrogen bond donor, steric role |
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 |
B | HIS287 | metal ligand |