4b6h

X-ray diffraction
2.6Å resolution

Structure of hDcp1a in complex with proline rich sequence of PNRC2

Released:

Function and Biology Details

Reaction catalysed:
5'-(N(7)-methylguanosine 5'-triphospho)-[mRNA] + H(2)O = N(7)-methylguanosine 5'-diphosphate + 5'-phospho-[mRNA]
Biochemical function:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
PDBe Complex ID:
PDB-CPX-192486 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
mRNA-decapping enzyme 1A Chains: A, B
Molecule details ›
Chains: A, B
Length: 134 amino acids
Theoretical weight: 15.49 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q9NPI6 (Residues: 1-130; Coverage: 22%)
Gene names: DCP1A, SMIF
Sequence domains: Dcp1-like decapping family
Structure domains: Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB)
Proline-rich nuclear receptor coactivator 2 Chains: C, D
Molecule details ›
Chains: C, D
Length: 135 amino acids
Theoretical weight: 15.13 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q9NPJ4 (Residues: 1-121; Coverage: 87%)
Gene names: HSPC208, PNRC2
Sequence domains: Proline-rich nuclear receptor coactivator motif

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-2
Spacegroup: I222
Unit cell:
a: 76.091Å b: 97.639Å c: 109.688Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.239 0.234 0.285
Expression system: Escherichia coli BL21