1NR5
Crystal structure of 3-dehydroquinate synthase (DHQS) in complex with ZN2+, NAD and carbaphosphonate
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 | 5 |
| Details | BINDING SITE FOR RESIDUE ZN A 600 |
| Chain | Residue |
| A | GLU194 |
| A | HIS271 |
| A | HIS287 |
| A | NAD400 |
| A | CRB1500 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN B 601 |
| Chain | Residue |
| B | CRB1501 |
| B | GLU194 |
| B | HIS271 |
| B | HIS287 |
| B | NAD401 |
| site_id | AC3 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE CO B 602 |
| Chain | Residue |
| B | ARG303 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL A 603 |
| Chain | Residue |
| A | LYS89 |
| A | LYS89 |
| A | HOH1622 |
| A | HOH1622 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL B 604 |
| Chain | Residue |
| B | LYS89 |
| B | LYS89 |
| B | HOH1608 |
| B | HOH1608 |
| site_id | AC6 |
| Number of Residues | 31 |
| 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 | LYS161 |
| A | PHE179 |
| A | THR182 |
| A | LEU183 |
| A | GLU187 |
| A | ASN190 |
| A | LYS250 |
| A | HIS287 |
| A | ZN600 |
| A | CRB1500 |
| A | HOH1506 |
| A | HOH1514 |
| A | HOH1525 |
| A | HOH1532 |
| A | HOH1539 |
| A | HOH1545 |
| A | HOH1570 |
| site_id | AC7 |
| Number of Residues | 30 |
| Details | BINDING SITE FOR RESIDUE NAD B 401 |
| Chain | Residue |
| B | ASP44 |
| B | ASN46 |
| B | GLU81 |
| B | LYS84 |
| B | GLY114 |
| B | GLY115 |
| B | VAL116 |
| B | ASP119 |
| B | THR139 |
| B | THR140 |
| B | ASP146 |
| B | SER147 |
| B | LYS152 |
| B | LYS161 |
| B | PHE179 |
| B | THR182 |
| B | LEU183 |
| B | GLU187 |
| B | ASN190 |
| B | GLU194 |
| B | LYS250 |
| B | HIS287 |
| B | ZN601 |
| B | CRB1501 |
| B | HOH1503 |
| B | HOH1508 |
| B | HOH1552 |
| B | HOH1566 |
| B | HOH1573 |
| B | HOH1577 |
| site_id | AC8 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE CRB A 1500 |
| Chain | Residue |
| A | ARG130 |
| A | ASP146 |
| A | LYS152 |
| A | ASN162 |
| A | GLU194 |
| A | LYS197 |
| A | LYS250 |
| A | ARG264 |
| A | LEU267 |
| A | ASN268 |
| A | HIS271 |
| A | HIS275 |
| A | HIS287 |
| A | LYS356 |
| A | NAD400 |
| A | ZN600 |
| A | HOH1522 |
| A | HOH1532 |
| A | HOH1534 |
| site_id | AC9 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE CRB B 1501 |
| Chain | Residue |
| B | ARG130 |
| B | ASP146 |
| B | LYS152 |
| B | ASN162 |
| B | GLU194 |
| B | LYS197 |
| B | LYS250 |
| B | ARG264 |
| B | LEU267 |
| B | ASN268 |
| B | HIS271 |
| B | HIS275 |
| B | HIS287 |
| B | LYS356 |
| B | NAD401 |
| B | ZN601 |
| B | HOH1503 |
| B | HOH1505 |
| B | HOH1532 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| 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 | 26 |
| 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 | 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 |
