PDBe 5kq1

X-ray diffraction
3Å resolution

Crystal structure of S. pombe Dcp1/Dcp2 in complex with H. sapiens PNRC2

Released:
Primary publication:
Structural basis of mRNA-cap recognition by Dcp1-Dcp2.
OpenAccess logo Nat. Struct. Mol. Biol. (2016)
PMID: 27694842

Function and Biology Details

Structure analysis Details

Assembly composition:
hetero hexamer (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
mRNA-decapping enzyme subunit 1 Chains: A, D
Molecule details ›
Chains: A, D
Length: 130 amino acids
Theoretical weight: 15.34 KDa
Source organism: Schizosaccharomyces pombe 972h-
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9P805 (Residues: 1-127; Coverage: 100%)
Gene names: SPBC3B9.21, dcp1
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, F
Molecule details ›
Chains: C, F
Length: 31 amino acids
Theoretical weight: 3.37 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9NPJ4 (Residues: 91-121; Coverage: 22%)
Gene names: HSPC208, PNRC2
Sequence domains: Proline-rich nuclear receptor coactivator motif
mRNA decapping complex subunit 2 Chains: B, E
Molecule details ›
Chains: B, E
Length: 249 amino acids
Theoretical weight: 28.95 KDa
Source organism: Schizosaccharomyces pombe 972h-
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: O13828 (Residues: 1-244; Coverage: 33%)
Gene names: SPAC19A8.12, dcp2
Sequence domains:

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.3.1
Spacegroup: P21
Unit cell:
a: 45.622Å b: 118.727Å c: 93.174Å
α: 90° β: 102.77° γ: 90°
R-values:
R R work R free
0.212 0.21 0.247
Expression system: Escherichia coli BL21(DE3)