› 1dhg

X-ray diffraction
2.5Å resolution

HG-SUBSTITUTED DESULFOREDOXIN

Released:
DOI: 10.2210/pdb1dhg/pdb
PDB entry 1dhg coloured by chain, front view.
PDB entry 1dhg coloured by chain, side view.
PDB entry 1dhg coloured by chain, top view.
Source organism: Megalodesulfovibrio gigas
Primary publication:
Structural studies by X-ray diffraction on metal substituted desulforedoxin, a rubredoxin-type protein.
Archer M, Carvalho AL, Teixeira S, Moura I, Moura JJ, Rusnak F, Romão MJ
Protein Sci 8 1536-45 (1999)
PMID: 10422844

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-132365 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Desulforedoxin Chains: A, B
Molecule details ›
Chains: A, B
Length: 36 amino acids
Theoretical weight: 3.81 KDa
Source organism: Megalodesulfovibrio gigas
Expression system: Escherichia coli
UniProt:
  • Canonical: P00273 (Residues: 2-37; Coverage: 97%)
Gene name: dsr
Sequence domains: Desulfoferrodoxin, N-terminal domain

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: ENRAF-NONIUS
Spacegroup: P3121
Unit cell:
a: 27.9Å b: 27.9Å c: 130.9Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.182 0.182 not available
Expression system: Escherichia coli

Quick links

Citations

9 citation in other articles

Metal-induced folding of a designed metalloprotein.
Kharenko et al. (2004)
8 more

1 mention without citation

N-terminal splicing extensions of the human MYO1C gene fine-tune the kinetics of the three full-length myosin IC isoforms.
Zattelman et al. (2017)