1SG6
Crystal structure of Aspergillus nidulans 3-dehydroquinate synthase (AnDHQS) in complex with Zn2+ and NAD+, at 1.7D
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 | 3 |
| Details | BINDING SITE FOR RESIDUE ZN A 1600 |
| Chain | Residue |
| 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 | 31 |
| Details | BINDING SITE FOR RESIDUE NAD A 1400 |
| Chain | Residue |
| 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 | HOH1603 |
| A | HOH1611 |
| A | HOH1612 |
| A | HOH1626 |
| A | HOH1638 |
| A | HOH1640 |
| A | HOH1651 |
| A | HOH1662 |
| A | HOH1680 |
| A | HOH1684 |
| A | HOH1812 |
| A | HOH1824 |
| A | HOH1914 |
| A | ASP44 |
| A | ASN46 |
| A | ILE47 |
| site_id | AC4 |
| Number of Residues | 30 |
| Details | BINDING SITE FOR RESIDUE NAD B 1401 |
| Chain | Residue |
| B | ASP44 |
| B | ASN46 |
| B | ILE47 |
| 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 | GLU187 |
| B | HOH1612 |
| B | HOH1613 |
| B | HOH1623 |
| B | HOH1625 |
| B | HOH1627 |
| B | HOH1691 |
| B | HOH1806 |
| B | HOH1818 |
| B | HOH1843 |
| B | HOH1888 |
| B | HOH1907 |
| B | HOH2031 |
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 | 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 |
