› 1t9q

X-ray diffraction
1.8Å resolution

Crystal Structure of V44L Cp Rubredoxin

Released:
DOI: 10.2210/pdb1t9q/pdb
PDB 1t9q coloured by chain and viewed from the front.
PDB 1t9q coloured by chain and viewed from the side.
PDB 1t9q coloured by chain and viewed from the top.
Source organism: Clostridium pasteurianum
Entry authors: Park IY, Eidsness MK, Lin IJ, Gebel EB, Youn B, Harley JL, Machonkin TE, Frederick RO, Markley JL, Smith ET, Ichiye T, Kang C

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Rubredoxin Chain: A
Molecule details ›
Chain: A
Length: 54 amino acids
Theoretical weight: 6.07 KDa
Source organism: Clostridium pasteurianum
Expression system: Escherichia coli
UniProt:
  • Canonical: P00268 (Residues: 1-54; Coverage: 100%)
Structure domains: Rubrerythrin, domain 2

Ligands and Environments

1 bound ligand:
Ligand FE 1 x FE
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 14-BM-C
Spacegroup: R3
Unit cell:
a: 63.77Å b: 63.77Å c: 32.76Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.211 0.206 0.228
Expression system: Escherichia coli

Quick links

Citations

9 citation in other articles

Changes in hydrogen-bond strengths explain reduction potentials in 10 rubredoxin variants.
Lin et al. (2005)
8 more