2DQB
Crystal structure of dNTP triphosphohydrolase from Thermus thermophilus HB8, which is homologous to dGTP triphosphohydrolase
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0006203 | biological_process | dGTP catabolic process |
A | 0008832 | molecular_function | dGTPase activity |
A | 0016787 | molecular_function | hydrolase activity |
A | 0016793 | molecular_function | triphosphoric monoester hydrolase activity |
A | 0046872 | molecular_function | metal ion binding |
B | 0006203 | biological_process | dGTP catabolic process |
B | 0008832 | molecular_function | dGTPase activity |
B | 0016787 | molecular_function | hydrolase activity |
B | 0016793 | molecular_function | triphosphoric monoester hydrolase activity |
B | 0046872 | molecular_function | metal ion binding |
C | 0006203 | biological_process | dGTP catabolic process |
C | 0008832 | molecular_function | dGTPase activity |
C | 0016787 | molecular_function | hydrolase activity |
C | 0016793 | molecular_function | triphosphoric monoester hydrolase activity |
C | 0046872 | molecular_function | metal ion binding |
D | 0006203 | biological_process | dGTP catabolic process |
D | 0008832 | molecular_function | dGTPase activity |
D | 0016787 | molecular_function | hydrolase activity |
D | 0016793 | molecular_function | triphosphoric monoester hydrolase activity |
D | 0046872 | molecular_function | metal ion binding |
E | 0006203 | biological_process | dGTP catabolic process |
E | 0008832 | molecular_function | dGTPase activity |
E | 0016787 | molecular_function | hydrolase activity |
E | 0016793 | molecular_function | triphosphoric monoester hydrolase activity |
E | 0046872 | molecular_function | metal ion binding |
F | 0006203 | biological_process | dGTP catabolic process |
F | 0008832 | molecular_function | dGTPase activity |
F | 0016787 | molecular_function | hydrolase activity |
F | 0016793 | molecular_function | triphosphoric monoester hydrolase activity |
F | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE MG E 501 |
Chain | Residue |
E | HIS108 |
E | HIS169 |
E | GLU170 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE MG B 502 |
Chain | Residue |
B | HIS108 |
B | HIS169 |
B | GLU170 |
B | HOH537 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG C 503 |
Chain | Residue |
C | ASP109 |
C | ASP196 |
C | TYR200 |
C | GLN63 |
C | HIS79 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG D 504 |
Chain | Residue |
D | HIS79 |
D | HIS108 |
D | ASP109 |
D | ASP196 |
D | HOH534 |
site_id | AC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG F 505 |
Chain | Residue |
F | HIS108 |
F | ASP109 |
F | ASN136 |
F | HIS169 |
F | GLU170 |
F | HOH526 |
site_id | AC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG A 506 |
Chain | Residue |
A | HIS79 |
A | HIS108 |
A | ASP109 |
A | ASP196 |
A | TYR200 |