› 3rdi

X-ray diffraction
2.95Å resolution

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

Released:
DOI: 10.2210/pdb3rdi/pdb
PDB 3rdi coloured by chain and viewed from the front.
PDB 3rdi coloured by chain and viewed from the side.
PDB 3rdi coloured by chain and viewed from the top.
Source organism: Escherichia coli K-12
Entry authors: Knapp J, White MA, Lee JC

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

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

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

Experiments and Validation Details

Entry percentile scores
X-ray source: MACSCIENCE
Spacegroup: P212121
Unit cell:
a: 46.16Å b: 92.75Å c: 104.89Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.219 0.197 0.276
Expression system: Escherichia coli

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