› 3nl9

X-ray diffraction
1.78Å resolution

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-109456 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
HAD family hydrolase Chain: A
Molecule details ›
Chain: A
Length: 171 amino acids
Theoretical weight: 19.4 KDa
Source organism: Exiguobacterium sibiricum 255-15
Expression system: Escherichia coli
UniProt:
  • Canonical: B1YMF4 (Residues: 1-170; Coverage: 100%)
Gene name: Exig_1061
Sequence domains: Phosphoribosyl-ATP pyrophosphohydrolase
Structure domains: putative ntp pyrophosphohydrolase like domain

Ligands and Environments

1 bound ligand:
Ligand EDO 2 x EDO
1 modified residue:
Ligand MSE 5 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.2.2
Spacegroup: C2
Unit cell:
a: 52.088Å b: 69.043Å c: 50.208Å
α: 90° β: 111.81° γ: 90°
R-values:
R R work R free
0.179 0.177 0.222
Expression system: Escherichia coli

Quick links

Citations

1 citations in other articles

New variants of known folds: do they bring new biology?
Koonin EV. (2010)

1 mention without citation

Structure of a putative NTP pyrophosphohydrolase: YP_001813558.1 from Exiguobacterium sibiricum 255-15.
Han et al. (2010)