4HK6
Crystal structure of Cordyceps militaris IDCase in complex with 5-nitro-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 | 0016831 | molecular_function | carboxy-lyase activity |
A | 0019748 | biological_process | secondary metabolic process |
A | 0046872 | molecular_function | metal ion binding |
A | 1901360 | biological_process | obsolete organic cyclic compound metabolic process |
B | 0005737 | cellular_component | cytoplasm |
B | 0005829 | cellular_component | cytosol |
B | 0016787 | molecular_function | hydrolase activity |
B | 0016831 | molecular_function | carboxy-lyase activity |
B | 0019748 | biological_process | secondary metabolic process |
B | 0046872 | molecular_function | metal ion binding |
B | 1901360 | biological_process | obsolete organic cyclic compound metabolic process |
C | 0005737 | cellular_component | cytoplasm |
C | 0005829 | cellular_component | cytosol |
C | 0016787 | molecular_function | hydrolase activity |
C | 0016831 | molecular_function | carboxy-lyase activity |
C | 0019748 | biological_process | secondary metabolic process |
C | 0046872 | molecular_function | metal ion binding |
C | 1901360 | biological_process | obsolete organic cyclic compound metabolic process |
D | 0005737 | cellular_component | cytoplasm |
D | 0005829 | cellular_component | cytosol |
D | 0016787 | molecular_function | hydrolase activity |
D | 0016831 | molecular_function | carboxy-lyase activity |
D | 0019748 | biological_process | secondary metabolic process |
D | 0046872 | molecular_function | metal ion binding |
D | 1901360 | biological_process | obsolete organic cyclic compound metabolic process |
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 | 5NU402 |
site_id | AC2 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE 5NU A 402 |
Chain | Residue |
A | HIS195 |
A | LEU218 |
A | PHE222 |
A | HIS251 |
A | ASP323 |
A | PHE326 |
A | PHE327 |
A | ZN401 |
A | HOH501 |
A | HIS14 |
A | LEU46 |
A | ARG68 |
A | ASN98 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN B 401 |
Chain | Residue |
B | HIS12 |
B | HIS14 |
B | HIS195 |
B | ASP323 |
B | 5NU402 |
site_id | AC4 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE 5NU B 402 |
Chain | Residue |
B | HIS12 |
B | HIS14 |
B | LEU46 |
B | ARG68 |
B | ASN98 |
B | HIS195 |
B | LEU218 |
B | PHE222 |
B | HIS251 |
B | ASP323 |
B | PHE326 |
B | PHE327 |
B | ZN401 |
B | HOH508 |
D | ARG262 |
site_id | AC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN C 401 |
Chain | Residue |
C | HIS12 |
C | HIS14 |
C | HIS195 |
C | ASP323 |
C | 5NU402 |
site_id | AC6 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE 5NU C 402 |
Chain | Residue |
A | ARG262 |
C | HIS12 |
C | HIS14 |
C | LEU46 |
C | ARG68 |
C | ASN98 |
C | HIS195 |
C | LEU218 |
C | PHE222 |
C | HIS251 |
C | ASP323 |
C | PHE326 |
C | PHE327 |
C | ZN401 |
site_id | AC7 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN D 401 |
Chain | Residue |
D | HIS12 |
D | HIS14 |
D | HIS195 |
D | ASP323 |
D | 5NU402 |
site_id | AC8 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE 5NU D 402 |
Chain | Residue |
B | ARG262 |
D | HIS12 |
D | HIS14 |
D | LEU46 |
D | ARG68 |
D | ASN98 |
D | HIS195 |
D | LEU218 |
D | PHE222 |
D | HIS251 |
D | ASP323 |
D | PHE326 |
D | PHE327 |
D | ZN401 |
D | HOH523 |