› 2jij

X-ray diffraction
2.9Å resolution

Crystal structure of the apo form of Chlamydomonas reinhardtii prolyl- 4 hydroxylase type I

Released:
DOI: 10.2210/pdb2jij/pdb
PDB entry 2jij coloured by chain, front view.
PDB entry 2jij coloured by chain, side view.
PDB entry 2jij coloured by chain, top view.
Source organism: Chlamydomonas reinhardtii
Primary publication:
The active site of an algal prolyl 4-hydroxylase has a large structural plasticity.
Koski MK, Hieta R, Böllner C, Kivirikko KI, Myllyharju J, Wierenga RK
J Biol Chem 282 37112-23 (2007)
PMID: 17940281

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-162777 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
PROLYL-4 HYDROXYLASE Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 233 amino acids
Theoretical weight: 26.15 KDa
Source organism: Chlamydomonas reinhardtii
Expression system: Escherichia coli
Structure domains: q2cbj1_9rhob like domain

Ligands and Environments

1 bound ligand:
Ligand CL 2 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-3
Spacegroup: P21212
Unit cell:
a: 98.32Å b: 117.46Å c: 72.04Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.214 0.212 0.261
Expression system: Escherichia coli

Quick links

Citations

8 review citations

Prolyl 4-hydroxylase.
Gorres et al. (2010)
7 more

4 mentions without citation

Prediction of novel families of enzymes involved in oxidative and other complex modifications of bases in nucleic acids.
Iyer et al. (2009)
3 more