› 1gmg

X-ray diffraction
1.9Å resolution

ALANINE 31 PROLINE MUTANT OF ROP PROTEIN, MONOCLINIC FORM

Released:
DOI: 10.2210/pdb1gmg/pdb
PDB entry 1gmg coloured by chain, front view.
PDB entry 1gmg coloured by chain, side view.
PDB entry 1gmg coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Structure determination of a small protein through a 23-dimensional molecular-replacement search.
Glykos NM, Kokkinidis M
Acta Crystallogr D Biol Crystallogr 59 709-18 (2003)
PMID: 12657790

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 Chains: A, B
Molecule details ›
Chains: A, B
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: RIGAKU RU300
Spacegroup: C2
Unit cell:
a: 94.39Å b: 24.25Å c: 64.53Å
α: 90° β: 130.4° γ: 90°
R-values:
R R work R free
0.187 0.187 0.232
Expression system: Escherichia coli

Quick links

Citations

4 citation in other articles

Structural polymorphism of a marginally stable 4-alpha-helical bundle. Images of a trapped molten globule?
Glykos et al. (2004)
3 more

1 mention without citation

Structural plasticity of 4-α-helical bundles exemplified by the puzzle-like molecular assembly of the Rop protein.
Amprazi et al. (2014)