› 4ccj

X-ray diffraction
2.15Å resolution

60S ribosomal protein L8 histidine hydroxylase (NO66) in apo form

Released:
DOI: 10.2210/pdb4ccj/pdb
PDB entry 4ccj coloured by chain, front view.
PDB entry 4ccj coloured by chain, side view.
PDB entry 4ccj coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Ribosomal oxygenases are structurally conserved from prokaryotes to humans.
Chowdhury R, Sekirnik R, Brissett NC, Krojer T, Ho CH, Ng SS, Clifton IJ, Ge W, Kershaw NJ, Fox GC, Muniz JRC, Vollmar M, Phillips C, Pilka ES, Kavanagh KL, von Delft F, Oppermann U, McDonough MA, Doherty AJ, Schofield CJ
Nature 510 422-426 (2014)
PMID: 24814345

Function and Biology Details

Reaction catalysed: 
(1a) a [histone H3]-N(6),N(6)-dimethyl-L-lysine(36) + 2-oxoglutarate + O(2) = a [histone H3]-N(6)-methyl-L-lysine(36) + succinate + formaldehyde + CO(2)
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-190649 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ribosomal oxygenase 1 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 467 amino acids
Theoretical weight: 53.24 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9H6W3 (Residues: 183-641; Coverage: 72%)
Gene names: C14orf169, MAPJD, NO66, RIOX1
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand EDO 3 x EDO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04-1
Spacegroup: P21
Unit cell:
a: 102.44Å b: 81.56Å c: 151.96Å
α: 90° β: 94.66° γ: 90°
R-values:
R R work R free
0.202 0.202 0.21
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

22 review citations

2-Oxoglutarate-Dependent Oxygenases.
Islam et al. (2018)
21 more

1 mention without citation

Pro-metastatic collagen lysyl hydroxylase dimer assemblies stabilized by Fe2+-binding.
Guo et al. (2018)