› 1rpo

X-ray diffraction
1.4Å resolution

RESTORED HEPTAD PATTERN CONTINUITY DOES NOT ALTER THE FOLDING OF A 4-ALPHA-HELICAL BUNDLE

Released:
DOI: 10.2210/pdb1rpo/pdb
PDB entry 1rpo coloured by chain, front view.
PDB entry 1rpo coloured by chain, side view.
PDB entry 1rpo coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Restored heptad pattern continuity does not alter the folding of a four-alpha-helix bundle.
Vlassi M, Steif C, Weber P, Tsernoglou D, Wilson KS, Hinz HJ, Kokkinidis M
Nat Struct Biol 1 706-16 (1994)
PMID: 7634075

Function and Biology Details

Biochemical function:
  • not assigned
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-136490 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Regulatory protein rop Chain: A
Molecule details ›
Chain: A
Length: 65 amino acids
Theoretical weight: 7.38 KDa
Source organism: Escherichia coli
Expression system: Not provided
UniProt:
  • Canonical: P03051 (Residues: 1-29, 30-30, 31-63; Coverage: 100%)
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
Spacegroup: C2
Unit cell:
a: 46.96Å b: 37.94Å c: 31.84Å
α: 90° β: 101.04° γ: 90°
R-values:
R R work R free
0.189 0.189 not available
Expression system: Not provided

Quick links

Citations

2 review citations

De novo design and structural characterization of proteins and metalloproteins.
DeGrado et al. (1999)
1 more

6 mentions without citation

Universality classes in folding times of proteins.
Cieplak et al. (2003)
5 more