› 5cro

X-ray diffraction
2.3Å resolution

REFINED STRUCTURE OF CRO REPRESSOR PROTEIN FROM BACTERIOPHAGE LAMBDA

Released:
DOI: 10.2210/pdb5cro/pdb
PDB entry 5cro coloured by chain, front view.
PDB entry 5cro coloured by chain, side view.
PDB entry 5cro coloured by chain, top view.
Source organism: Escherichia virus Lambda
Primary publication:
Refined structure of Cro repressor protein from bacteriophage lambda suggests both flexibility and plasticity.
Ohlendorf DH, Tronrud DE, Matthews BW
J Mol Biol 280 129-36 (1998)
PMID: 9653036

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
homo dimer (preferred)
homo 24-mer
homo tetramer
Assembly name:
PDBe Complex ID:
PDB-CPX-136477 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Regulatory protein cro Chains: A, B, C, O
Molecule details ›
Chains: A, B, C, O
Length: 66 amino acids
Theoretical weight: 7.38 KDa
Source organism: Escherichia virus Lambda
UniProt:
  • Canonical: P03040 (Residues: 1-66; Coverage: 100%)
Gene names: cro, lambdap57
Sequence domains: Cro
Structure domains: CRO Repressor

Ligands and Environments

1 bound ligand:
Ligand PO4 2 x PO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ELLIOTT GX-21
Spacegroup: R32
Unit cell:
a: 91.6Å b: 91.6Å c: 268.5Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.193 0.193 not available

Quick links

Citations

29 citation in other articles

The subunit interfaces of weakly associated homodimeric proteins.
Dey et al. (2010)
28 more

17 mentions without citation

Interplay of self-association and conformational flexibility in regulating protein function.
Garton et al. (2018)
16 more