› 3veg

X-ray diffraction
2.35Å resolution

Rhodococcus jostii RHA1 DypB R244L variant in complex with heme

Released:
DOI: 10.2210/pdb3veg/pdb
PDB entry 3veg coloured by chain, front view.
PDB entry 3veg coloured by chain, side view.
PDB entry 3veg coloured by chain, top view.
Source organism: Rhodococcus jostii RHA1
Primary publication:
Distal heme pocket residues of B-type dye-decolorizing peroxidase: arginine but not aspartate is essential for peroxidase activity.
Singh R, Grigg JC, Armstrong Z, Murphy MEP, Eltis LD
J Biol Chem 287 10623-10630 (2012)
PMID: 22308037

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo hexamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-171142 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Iron-dependent peroxidase Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 353 amino acids
Theoretical weight: 37.49 KDa
Source organism: Rhodococcus jostii RHA1
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q0SE24 (Residues: 1-350; Coverage: 100%)
Gene name: RHA1_ro02407
Sequence domains:

Ligands and Environments

2 bound ligands:
Ligand HEM 3 x HEM
Ligand CL 3 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: CLSI BEAMLINE 08B1-1
Spacegroup: P3221
Unit cell:
a: 133.224Å b: 133.224Å c: 158.922Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.188 0.186 0.222
Expression system: Escherichia coli BL21

Quick links

Citations

9 review citations

Exploring bacterial lignin degradation.
Brown et al. (2014)
8 more

4 mentions without citation

Substrate, product, and cofactor: The extraordinarily flexible relationship between the CDE superfamily and heme.
Celis et al. (2015)
3 more