› 3rj2

X-ray diffraction
2.2Å resolution

Structural and functional characterization of a novel histone H3 binding protein ORF158L from the Singapore grouper iridovirus (SGIV)

Released:
DOI: 10.2210/pdb3rj2/pdb
PDB entry 3rj2 coloured by chain, front view.
PDB entry 3rj2 coloured by chain, side view.
PDB entry 3rj2 coloured by chain, top view.
Source organism: Singapore grouper iridovirus
Primary publication:
Novel histone H3 binding protein ORF158L from the Singapore grouper iridovirus.
Tran BN, Chen L, Liu Y, Wu J, Velázquez-Campoy A, Sivaraman J, Hew CL
J Virol 85 9159-66 (2011)
PMID: 21715494

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-178533 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Putative uncharacterized protein Chain: X
Molecule details ›
Chain: X
Length: 138 amino acids
Theoretical weight: 15.8 KDa
Source organism: Singapore grouper iridovirus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q5YFA7 (Residues: 1-138; Coverage: 100%)
Gene name: ORF158L
Sequence domains: Histone H3 binding protein ORF158L-like
Structure domains: Jelly Rolls

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X29A
Spacegroup: C2
Unit cell:
a: 60.066Å b: 41.002Å c: 52.386Å
α: 90° β: 95.33° γ: 90°
R-values:
R R work R free
0.201 0.197 0.275
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Host-virus interactions: from the perspectives of epigenetics.
Li et al. (2014)
4 other articles

1 mention without citation

Novel histone H3 binding protein ORF158L from the Singapore grouper iridovirus.
Tran et al. (2011)