Function and Biology Details
Reactions catalysed:
5'-(N(7)-methylguanosine 5'-triphospho)-[mRNA] + H(2)O = N(7)-methylguanosine 5'-diphosphate + 5'-phospho-[mRNA]
IDP + H(2)O = IMP + phosphate
Biochemical function:
- not assigned
Biological process:
- not assigned
Cellular component:
- not assigned
Structure analysis Details
Assembly composition:
hetero tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-171429 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
U8 snoRNA-decapping enzyme
Molecule details ›
Chains: A, B
Length: 196 amino acids
Theoretical weight: 21.54 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Sequence domains: NUDIX domain
Structure domains: Nucleoside Triphosphate Pyrophosphohydrolase
Length: 196 amino acids
Theoretical weight: 21.54 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical:
Q96DE0 (Residues: 1-104, 105-195; Coverage: 100%)
Sequence domains: NUDIX domain
Structure domains: Nucleoside Triphosphate Pyrophosphohydrolase
TP53-binding protein 1
Molecule details ›
Chains: C, D
Length: 123 amino acids
Theoretical weight: 13.94 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Sequence domains: Tumour suppressor p53-binding protein-1 Tudor
Structure domains:
Length: 123 amino acids
Theoretical weight: 13.94 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical: Q12888 (Residues: 1484-1603; Coverage: 6%)
Sequence domains: Tumour suppressor p53-binding protein-1 Tudor
Structure domains:
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
X-ray source:
APS BEAMLINE 19-ID
Spacegroup:
P43212
Expression system: Escherichia coli
