› 1vqj

X-ray diffraction
1.8Å resolution

GENE V PROTEIN MUTANT WITH VAL 35 REPLACED BY ILE 35 (V35I)

Released:
DOI: 10.2210/pdb1vqj/pdb
PDB entry 1vqj coloured by chain, front view.
PDB entry 1vqj coloured by chain, side view.
PDB entry 1vqj coloured by chain, top view.
Source organism: Enterobacteria phage f1
Primary publication:
Context dependence of mutational effects in a protein: the crystal structures of the V35I, I47V and V35I/I47V gene V protein core mutants.
Zhang H, Skinner MM, Sandberg WS, Wang AH, Terwilliger TC
J Mol Biol 259 148-59 (1996)
PMID: 8648642

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-159614 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
DNA-Binding protein G5P Chain: A
Molecule details ›
Chain: A
Length: 87 amino acids
Theoretical weight: 9.71 KDa
Source organism: Enterobacteria phage f1
Expression system: Escherichia coli
UniProt:
  • Canonical: P69543 (Residues: 1-87; Coverage: 100%)
Gene name: V
Sequence domains: Helix-destabilising protein
Structure domains: Nucleic acid-binding proteins

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: C2
Unit cell:
a: 76.14Å b: 28.11Å c: 42.56Å
α: 90° β: 103.42° γ: 90°
R-values:
R R work R free
0.206 0.206 not available
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Stabilization of protein structures.
Lee et al. (1997)
1 more

1 mention without citation

Thoroughly sampling sequence space: large-scale protein design of structural ensembles.
Larson et al. (2002)