2HK7
Crystal structure of shikimate dehydrogenase from aquifex aeolicus in complex with mercury at 2.5 angstrom resolution
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004764 | molecular_function | shikimate 3-dehydrogenase (NADP+) 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 | 0016491 | molecular_function | oxidoreductase activity |
| A | 0019632 | biological_process | shikimate metabolic process |
| A | 0050661 | molecular_function | NADP binding |
| B | 0004764 | molecular_function | shikimate 3-dehydrogenase (NADP+) activity |
| B | 0005829 | cellular_component | cytosol |
| B | 0008652 | biological_process | amino acid biosynthetic process |
| B | 0009073 | biological_process | aromatic amino acid family biosynthetic process |
| B | 0009423 | biological_process | chorismate biosynthetic process |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0019632 | biological_process | shikimate metabolic process |
| B | 0050661 | molecular_function | NADP binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE HG A 270 |
| Chain | Residue |
| A | HIS18 |
| A | HOH321 |
| A | HOH322 |
| site_id | AC2 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE HG A 271 |
| Chain | Residue |
| A | MET1 |
| site_id | AC3 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE HG A 272 |
| Chain | Residue |
| A | CYS253 |
| site_id | AC4 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE HG B 270 |
| Chain | Residue |
| B | HIS18 |
| site_id | AC5 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE HG B 271 |
| Chain | Residue |
| B | MET1 |
| site_id | AC6 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE HG B 272 |
| Chain | Residue |
| B | CYS253 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_00222","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"17649975","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 26 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00222","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"17649975","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00222","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 10 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00222","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"17649975","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1nvt |
| Chain | Residue | Details |
| A | ASN97 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1nvt |
| Chain | Residue | Details |
| B | ASN97 |
