1NVF
Crystal structure of 3-dehydroquinate synthase (DHQS) in complex with ZN2+, ADP 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 |
| 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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 600 |
| Chain | Residue |
| A | GLU194 |
| A | HIS271 |
| A | HIS287 |
| A | CRB500 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 601 |
| Chain | Residue |
| B | GLU194 |
| B | HIS271 |
| B | HIS287 |
| B | CRB501 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN C 602 |
| Chain | Residue |
| C | GLU194 |
| C | HIS271 |
| C | HIS287 |
| C | CRB502 |
| C | ASP146 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL C 603 |
| Chain | Residue |
| C | LYS89 |
| C | LYS89 |
| C | HOH2610 |
| C | HOH2610 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL A 604 |
| Chain | Residue |
| A | LYS89 |
| B | LYS89 |
| B | HOH629 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL C 2605 |
| Chain | Residue |
| C | ARG231 |
| C | HOH2698 |
| C | HOH2781 |
| site_id | AC7 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE ADP A 400 |
| Chain | Residue |
| A | ASP44 |
| A | ASN46 |
| A | ILE47 |
| A | GLY114 |
| A | GLY115 |
| A | VAL116 |
| A | THR139 |
| A | THR140 |
| A | PHE179 |
| A | THR182 |
| A | LEU183 |
| A | GLU187 |
| A | ASN190 |
| A | HOH619 |
| A | HOH670 |
| A | HOH676 |
| site_id | AC8 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE ADP B 401 |
| Chain | Residue |
| B | ASP44 |
| B | ASN46 |
| B | ILE47 |
| B | PRO79 |
| B | GLY114 |
| B | GLY115 |
| B | VAL116 |
| B | THR139 |
| B | THR140 |
| B | LEU142 |
| B | PHE179 |
| B | THR182 |
| B | LEU183 |
| B | GLU187 |
| B | ASN190 |
| site_id | AC9 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE ADP C 402 |
| Chain | Residue |
| C | ASP44 |
| C | ASN46 |
| C | ILE47 |
| C | GLY114 |
| C | GLY115 |
| C | VAL116 |
| C | THR139 |
| C | THR140 |
| C | LEU142 |
| C | PHE179 |
| C | THR182 |
| C | LEU183 |
| C | GLU187 |
| C | ASN190 |
| C | HOH2741 |
| site_id | BC1 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE CRB A 500 |
| Chain | Residue |
| 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 | ZN600 |
| B | ARG130 |
| site_id | BC2 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE CRB B 501 |
| Chain | Residue |
| A | 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 | ZN601 |
| site_id | BC3 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE CRB C 502 |
| Chain | Residue |
| C | ARG130 |
| C | ASP146 |
| C | LYS152 |
| C | ASN162 |
| C | GLU194 |
| C | LYS197 |
| C | LYS250 |
| C | ARG264 |
| C | LEU267 |
| C | ASN268 |
| C | HIS271 |
| C | HIS275 |
| C | HIS287 |
| C | LYS356 |
| C | ZN602 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| 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 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 33 |
| 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 | |
| A | ASP119 | |
| A | THR139 | |
| A | LYS161 | |
| A | PHE179 | |
| A | ASN190 | |
| A | GLU194 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 21 |
| 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 | |
| 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 | 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 |
