› 5qp9

X-ray diffraction
1.72Å resolution

PanDDA analysis group deposition -- Crystal Structure of DCP2 (NUDT20) in complex with Z100435060

Released:
DOI: 10.2210/pdb5qp9/pdb
PDB 5qp9 coloured by chain and viewed from the front.
PDB 5qp9 coloured by chain and viewed from the side.
PDB 5qp9 coloured by chain and viewed from the top.
Source organism: Homo sapiens
Entry authors: Nelson ER, Velupillai S, Talon R, Collins PM, Krojer T, Wang D, Brandao-Neto J, Douangamath A, Burgess-Brown N, Arrowsmith CH, Bountra C, Huber K, von Delft F

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:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
m7GpppN-mRNA hydrolase Chain: A
Molecule details ›
Chain: A
Length: 167 amino acids
Theoretical weight: 19.07 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8IU60 (Residues: 95-260; Coverage: 40%)
Gene names: DCP2, NUDT20
Sequence domains: NUDIX domain
Structure domains: Nucleoside Triphosphate Pyrophosphohydrolase

Ligands and Environments

4 bound ligands:
Ligand EDO 2 x EDO
Ligand DMS 1 x DMS
Ligand ACT 2 x ACT
Ligand LJD 1 x LJD
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04-1
Spacegroup: P212121
Unit cell:
a: 48.406Å b: 60.406Å c: 65.58Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.204 0.202 0.253
Expression system: Escherichia coli

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