1q67

X-ray diffraction
2.3Å resolution

Crystal structure of Dcp1p

Released:
Source organism: Saccharomyces cerevisiae
Primary publication:
Crystal structure of Dcp1p and its functional implications in mRNA decapping.
Nat. Struct. Mol. Biol. 11 249-56 (2004)
PMID: 14758354

Function and Biology Details

Biochemical function:
Cellular component:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
mRNA-decapping enzyme subunit 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 231 amino acids
Theoretical weight: 26.29 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli
UniProt:
  • Canonical: Q12517 (Residues: 1-231; Coverage: 100%)
Gene names: DCP1, YOL149W
Sequence domains: Dcp1-like decapping family
Structure domains: Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB)

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL41XU
Spacegroup: P321
Unit cell:
a: 123.55Å b: 123.55Å c: 77.9Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.227 0.227 0.268
Expression system: Escherichia coli