› 1qcv

Solution NMR

RUBREDOXIN VARIANT (PFRD-XC4) FOLDS WITHOUT IRON

Released:
DOI: 10.2210/pdb1qcv/pdb
PDB entry 1qcv coloured by chain, ensemble of 29 models, front view.
PDB entry 1qcv coloured by chain, ensemble of 29 models, side view.
PDB entry 1qcv coloured by chain, ensemble of 29 models, top view.
Source organism: Pyrococcus furiosus
Primary publication:
Contribution of surface salt bridges to protein stability.
Strop P, Mayo SL
Biochemistry 39 1251-5 (2000)
PMID: 10684603

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-150200 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Rubredoxin Chain: A
Molecule details ›
Chain: A
Length: 53 amino acids
Theoretical weight: 5.87 KDa
Source organism: Pyrococcus furiosus
Expression system: Escherichia coli
UniProt:
  • Canonical: P24297 (Residues: 2-54; Coverage: 98%)
Gene names: PF1282, rub
Sequence domains: Rubredoxin
Structure domains: Rubrerythrin, domain 2

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: distance geometry
Expression system: Escherichia coli

Quick links

Citations

10 review citations

Rational engineering of enzyme stability.
Eijsink et al. (2004)
9 more

1 mention without citation

Effective approach for calculations of absolute stability of proteins using focused dielectric constants.
Vicatos et al. (2009)