› 3k79

X-ray diffraction
1.96Å resolution

C38A, C52V Cysteine-Free Variant of Rop (Rom)

Released:
DOI: 10.2210/pdb3k79/pdb
PDB entry 3k79 coloured by chain, front view.
PDB entry 3k79 coloured by chain, side view.
PDB entry 3k79 coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Cysteine-free Rop: a four-helix bundle core mutant has wild-type stability and structure but dramatically different unfolding kinetics.
Hari SB, Byeon C, Lavinder JJ, Magliery TJ
Protein Sci 19 670-9 (2010)
PMID: 20095056

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-136490 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Regulatory protein rop Chain: A
Molecule details ›
Chain: A
Length: 63 amino acids
Theoretical weight: 7.13 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P03051 (Residues: 2-63; Coverage: 98%)
Gene name: rop
Sequence domains: Rop protein
Structure domains: Helix Hairpins

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH3R
Spacegroup: C2
Unit cell:
a: 44.664Å b: 40.304Å c: 31.666Å
α: 90° β: 101.97° γ: 90°
R-values:
R R work R free
0.167 0.163 0.25
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Energetics of oligomeric protein folding and association.
Doyle et al. (2013)
8 other articles

1 mention without citation

Cysteine-free Rop: a four-helix bundle core mutant has wild-type stability and structure but dramatically different unfolding kinetics.
Hari et al. (2010)