PDBe 1fw4

X-ray diffraction
1.7Å resolution

CRYSTAL STRUCTURE OF E. COLI FRAGMENT TR2C FROM CALMODULIN TO 1.7 A RESOLUTION

Released:
Source organism: Bos taurus
Primary publication:
Structure of Escherichia coli fragment TR2C from calmodulin to 1.7 A resolution.
Acta Crystallogr. D Biol. Crystallogr. 57 664-9 (2001)
PMID: 11320306

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Calmodulin Chain: A
Molecule details ›
Chain: A
Length: 71 amino acids
Theoretical weight: 8.16 KDa
Source organism: Bos taurus
Expression system: Escherichia coli
UniProt:
  • Canonical: P62157 (Residues: 79-149; Coverage: 48%)
Gene names: CALM, CAM
Sequence domains: EF-hand domain pair
Structure domains: EF-hand

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: I41
Unit cell:
a: 37.802Å b: 37.802Å c: 99.779Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.218 0.218 0.22
Expression system: Escherichia coli