› 1b6q

X-ray diffraction
1.8Å resolution

ALANINE 31 PROLINE MUTANT OF ROP PROTEIN

Released:
DOI: 10.2210/pdb1b6q/pdb
PDB entry 1b6q coloured by chain, front view.
PDB entry 1b6q coloured by chain, side view.
PDB entry 1b6q coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Protein plasticity to the extreme: changing the topology of a 4-alpha-helical bundle with a single amino acid substitution.
Glykos NM, Cesareni G, Kokkinidis M
Structure 7 597-603 (1999)
PMID: 10404589

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-136490 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Regulatory protein rop Chain: A
Molecule details ›
Chain: A
Length: 63 amino acids
Theoretical weight: 7.26 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P03051 (Residues: 1-63; 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
X-ray source: OTHER
Spacegroup: C2221
Unit cell:
a: 30.4Å b: 42.1Å c: 81.4Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.189 0.189 0.24
Expression system: Escherichia coli

Quick links

Citations

8 review citations

De novo design of helical bundles as models for understanding protein folding and function.
Hill et al. (2000)
7 more

4 mentions without citation

Bhageerath: an energy based web enabled computer software suite for limiting the search space of tertiary structures of small globular proteins.
Jayaram et al. (2006)
3 more