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 | 8 |
Details | ACT_SITE: Proton acceptor; for 3-dehydroquinate synthase activity |
Chain | Residue | Details |
A | GLU260 | |
A | HIS275 | |
B | GLU260 | |
B | HIS275 | |
C | GLU260 | |
C | HIS275 | |
D | GLU260 | |
D | HIS275 |
site_id | SWS_FT_FI2 |
Number of Residues | 44 |
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 | |
C | ASP44 | |
C | GLU81 | |
C | GLY114 | |
C | ASP119 | |
C | THR139 | |
C | LYS161 | |
C | PHE179 | |
A | GLY114 | |
C | ASN190 | |
C | GLU194 | |
C | HIS271 | |
C | HIS287 | |
D | ASP44 | |
D | GLU81 | |
D | GLY114 | |
D | ASP119 | |
D | THR139 | |
D | LYS161 | |
A | ASP119 | |
D | PHE179 | |
D | ASN190 | |
D | GLU194 | |
D | HIS271 | |
D | HIS287 | |
A | THR139 | |
A | LYS161 | |
A | PHE179 | |
A | ASN190 | |
A | GLU194 |
site_id | SWS_FT_FI3 |
Number of Residues | 28 |
Details | BINDING: |
Chain | Residue | Details |
A | ARG130 | |
B | LYS152 | |
B | ASN162 | |
B | LYS250 | |
B | ARG264 | |
B | LYS356 | |
C | ARG130 | |
C | ASP146 | |
C | LYS152 | |
C | ASN162 | |
C | LYS250 | |
A | ASP146 | |
C | ARG264 | |
C | LYS356 | |
D | ARG130 | |
D | ASP146 | |
D | LYS152 | |
D | ASN162 | |
D | LYS250 | |
D | ARG264 | |
D | LYS356 | |
A | LYS152 | |
A | ASN162 | |
A | LYS250 | |
A | ARG264 | |
A | LYS356 | |
B | ARG130 | |
B | ASP146 |
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 | 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 |
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 |