1NVE
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 |
| C | 0003856 | molecular_function | 3-dehydroquinate synthase activity |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0009073 | biological_process | aromatic amino acid family biosynthetic process |
| C | 0016838 | molecular_function | carbon-oxygen lyase activity, acting on phosphates |
| D | 0003856 | molecular_function | 3-dehydroquinate synthase activity |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0009073 | biological_process | aromatic amino acid family biosynthetic process |
| D | 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 | ASP146 |
| B | GLU194 |
| B | HIS271 |
| B | HIS287 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN C 602 |
| Chain | Residue |
| C | GLU194 |
| C | HIS271 |
| C | HIS287 |
| C | ASP146 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN D 1603 |
| Chain | Residue |
| D | ASP146 |
| D | GLU194 |
| D | HIS271 |
| D | HIS287 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL A 604 |
| Chain | Residue |
| A | LYS89 |
| B | LYS89 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL C 1605 |
| Chain | Residue |
| C | LYS89 |
| D | LYS89 |
| D | HOH1686 |
| site_id | AC7 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE NAD A 400 |
| Chain | Residue |
| A | ASP44 |
| A | ASN46 |
| A | ILE47 |
| 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 | PRO184 |
| A | GLU187 |
| A | HOH714 |
| A | HOH732 |
| A | HOH759 |
| site_id | AC8 |
| Number of Residues | 26 |
| 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 | HOH607 |
| B | HOH608 |
| B | HOH638 |
| B | HOH647 |
| B | HOH663 |
| B | HOH727 |
| site_id | AC9 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE NAD C 402 |
| Chain | Residue |
| C | ASP44 |
| C | ASN46 |
| C | ILE47 |
| C | GLU81 |
| C | LYS84 |
| C | GLY114 |
| C | GLY115 |
| C | VAL116 |
| C | ASP119 |
| C | THR139 |
| C | THR140 |
| C | LEU142 |
| C | ASP146 |
| C | SER147 |
| C | LYS152 |
| C | PHE179 |
| C | THR182 |
| C | LEU183 |
| C | GLU187 |
| C | HOH1608 |
| C | HOH1616 |
| C | HOH1618 |
| C | HOH1735 |
| site_id | BC1 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE NAD D 1403 |
| Chain | Residue |
| D | GLY115 |
| D | VAL116 |
| D | ASP119 |
| D | THR139 |
| D | THR140 |
| D | ASP146 |
| D | SER147 |
| D | LYS152 |
| D | ASN162 |
| D | PHE179 |
| D | THR182 |
| D | LEU183 |
| D | PRO184 |
| D | GLU187 |
| D | HOH1626 |
| D | HOH1698 |
| D | ASP44 |
| D | ASN46 |
| D | ILE47 |
| D | GLU81 |
| D | LYS84 |
| D | GLY114 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 7 |
| Details | Active site: {"description":"Proton acceptor; for 3-dehydroquinate synthase activity"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 68 |
| 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 | 48 |
| 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 | CSA3 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1dqs |
| Chain | Residue | Details |
| C | HIS275 |
| site_id | CSA4 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1dqs |
| Chain | Residue | Details |
| D | 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 | 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 |
| site_id | MCSA3 |
| Number of Residues | 10 |
| Details | M-CSA 59 |
| Chain | Residue | Details |
| C | ARG130 | electrostatic stabiliser |
| C | HIS287 | metal ligand |
| C | LYS152 | hydrogen bond donor, steric role |
| C | GLU194 | metal ligand |
| C | LYS250 | electrostatic stabiliser, hydrogen bond donor, steric role |
| C | GLU260 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| C | ARG264 | electrostatic stabiliser, hydrogen bond donor, steric role |
| C | ASN268 | hydrogen bond donor, steric role |
| C | HIS271 | metal ligand |
| C | HIS275 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| site_id | MCSA4 |
| Number of Residues | 10 |
| Details | M-CSA 59 |
| Chain | Residue | Details |
| D | ARG130 | electrostatic stabiliser |
| D | HIS287 | metal ligand |
| D | LYS152 | hydrogen bond donor, steric role |
| D | GLU194 | metal ligand |
| D | LYS250 | electrostatic stabiliser, hydrogen bond donor, steric role |
| D | GLU260 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| D | ARG264 | electrostatic stabiliser, hydrogen bond donor, steric role |
| D | ASN268 | hydrogen bond donor, steric role |
| D | HIS271 | metal ligand |
| D | HIS275 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
