4HK7
Crystal structure of Cordyceps militaris IDCase in complex with uracil
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016829 | molecular_function | lyase activity |
| A | 0016831 | molecular_function | carboxy-lyase activity |
| A | 0019748 | biological_process | secondary metabolic process |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0016829 | molecular_function | lyase activity |
| B | 0016831 | molecular_function | carboxy-lyase activity |
| B | 0019748 | biological_process | secondary metabolic process |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0005829 | cellular_component | cytosol |
| C | 0016787 | molecular_function | hydrolase activity |
| C | 0016829 | molecular_function | lyase activity |
| C | 0016831 | molecular_function | carboxy-lyase activity |
| C | 0019748 | biological_process | secondary metabolic process |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0005829 | cellular_component | cytosol |
| D | 0016787 | molecular_function | hydrolase activity |
| D | 0016829 | molecular_function | lyase activity |
| D | 0016831 | molecular_function | carboxy-lyase activity |
| D | 0019748 | biological_process | secondary metabolic process |
| D | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN A 401 |
| Chain | Residue |
| A | HIS12 |
| A | HIS14 |
| A | HIS195 |
| A | ASP323 |
| A | URA403 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 402 |
| Chain | Residue |
| A | HIS379 |
| A | HIS384 |
| C | HIS379 |
| C | HIS381 |
| site_id | AC3 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE URA A 403 |
| Chain | Residue |
| A | HIS14 |
| A | ARG68 |
| A | ASN98 |
| A | HIS195 |
| A | LEU218 |
| A | PHE222 |
| A | ASP323 |
| A | PHE326 |
| A | ZN401 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN B 401 |
| Chain | Residue |
| B | HIS12 |
| B | HIS14 |
| B | HIS195 |
| B | ASP323 |
| B | URA402 |
| site_id | AC5 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE URA B 402 |
| Chain | Residue |
| B | HIS14 |
| B | LEU46 |
| B | ARG68 |
| B | ASN98 |
| B | HIS195 |
| B | PHE222 |
| B | ASP323 |
| B | PHE326 |
| B | ZN401 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN C 401 |
| Chain | Residue |
| C | HIS12 |
| C | HIS14 |
| C | HIS195 |
| C | ASP323 |
| C | URA402 |
| site_id | AC7 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE URA C 402 |
| Chain | Residue |
| C | HIS14 |
| C | ARG68 |
| C | ASN98 |
| C | HIS195 |
| C | LEU218 |
| C | PHE222 |
| C | ASP323 |
| C | PHE326 |
| C | ZN401 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN D 401 |
| Chain | Residue |
| D | HIS12 |
| D | HIS14 |
| D | HIS195 |
| D | ASP323 |
| D | URA403 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN D 402 |
| Chain | Residue |
| B | HIS379 |
| B | HIS381 |
| B | HOH519 |
| D | HIS379 |
| D | HIS384 |
| site_id | BC1 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE URA D 403 |
| Chain | Residue |
| D | HIS14 |
| D | ARG68 |
| D | ASN98 |
| D | HIS195 |
| D | LEU218 |
| D | PHE222 |
| D | ASP323 |
| D | PHE326 |
| D | ZN401 |
