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 | 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 | 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 |