3qop

X-ray diffraction
1.96Å resolution

Domain-domain flexibility leads to allostery within the camp receptor protein (CRP)

Released:
Source organism: Escherichia coli K-12
Entry authors: Knapp J, White MA, Lee JC

Function and Biology Details

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
cAMP-activated global transcriptional regulator CRP Chains: A, B
Molecule details ›
Chains: A, B
Length: 210 amino acids
Theoretical weight: 23.73 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
UniProt:
  • Canonical: P0ACJ8 (Residues: 1-210; Coverage: 100%)
Gene names: JW5702, b3357, cap, crp, csm
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL7-1
Spacegroup: P21
Unit cell:
a: 45.82Å b: 101.55Å c: 54.95Å
α: 90° β: 111.37° γ: 90°
R-values:
R R work R free
0.219 0.219 0.244
Expression system: Escherichia coli