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 |
