2EGZ
Crystal structure of the 3-dehydroquinate dehydratase from Aquifex aeolicus VF5
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003855 | molecular_function | 3-dehydroquinate dehydratase activity |
| A | 0005829 | cellular_component | cytosol |
| A | 0008652 | biological_process | amino acid biosynthetic process |
| A | 0009073 | biological_process | aromatic amino acid family biosynthetic process |
| A | 0009423 | biological_process | chorismate biosynthetic process |
| A | 0016829 | molecular_function | lyase activity |
| A | 0046279 | biological_process | 3,4-dihydroxybenzoate biosynthetic process |
| C | 0003855 | molecular_function | 3-dehydroquinate dehydratase activity |
| C | 0005829 | cellular_component | cytosol |
| C | 0008652 | biological_process | amino acid biosynthetic process |
| C | 0009073 | biological_process | aromatic amino acid family biosynthetic process |
| C | 0009423 | biological_process | chorismate biosynthetic process |
| C | 0016829 | molecular_function | lyase activity |
| C | 0046279 | biological_process | 3,4-dihydroxybenzoate biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE TLA C 5988 |
| Chain | Residue |
| C | ARG30 |
| C | ARG61 |
| C | HIS116 |
| C | LYS142 |
| C | ILE170 |
| C | MET172 |
| C | ARG180 |
| C | TYR192 |
| C | HOH6034 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE TLA A 4988 |
| Chain | Residue |
| A | ARG30 |
| A | ARG61 |
| A | HIS116 |
| A | LYS142 |
| A | ILE170 |
| A | MET172 |
| A | ARG180 |
| A | TYR192 |
| A | HOH5065 |
Functional Information from PROSITE/UniProt
| site_id | PS01028 |
| Number of Residues | 30 |
| Details | DEHYDROQUINASE_I Dehydroquinase class I active site. DIELssrgllvklynitkeagkk.LIiSYHN |
| Chain | Residue | Details |
| A | ASP88-ASN117 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_00214","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"23396056","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Schiff-base intermediate with substrate","evidences":[{"source":"HAMAP-Rule","id":"MF_00214","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"23396056","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00214","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00214","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"23396056","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1qfe |
| Chain | Residue | Details |
| A | LYS142 | |
| A | GLU65 | |
| A | HIS116 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1qfe |
| Chain | Residue | Details |
| C | LYS142 | |
| C | GLU65 | |
| C | HIS116 |
