2c46

X-ray diffraction
1.6Å resolution

CRYSTAL STRUCTURE OF THE HUMAN RNA guanylyltransferase and 5'- phosphatase

Released:
Source organism: Homo sapiens
Entry authors: Debreczeni J, Johansson C, Longman E, Gileadi O, SavitskySmee P, Smee C, Bunkoczi G, Ugochukwu E, von Delft F, Sundstrom M, Weigelt J, Arrowsmith C, Edwards A, Knapp S

Function and Biology Details

Reactions catalysed:
GTP + a 5'-diphospho-[mRNA] = diphosphate + a 5'-(5'-triphosphoguanosine)-[mRNA]
A 5'-triphospho-[mRNA] + H(2)O = a 5'-diphospho-[mRNA] + phosphate
Biochemical function:
  • not assigned
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assemblies composition:
homo tetramer
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-130222 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
mRNA-capping enzyme Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 241 amino acids
Theoretical weight: 27.69 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: O60942 (Residues: 1-219; Coverage: 37%)
Gene names: CAP1A, RNGTT
Sequence domains: Dual specificity phosphatase, catalytic domain
Structure domains: Protein tyrosine phosphatase superfamily

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X10SA
Spacegroup: P21
Unit cell:
a: 60.4Å b: 161.6Å c: 60.7Å
α: 90° β: 104.7° γ: 90°
R-values:
R R work R free
0.206 0.204 0.234
Expression system: Escherichia coli BL21