› 1cnr

X-ray diffraction
1.05Å resolution

CORRELATED DISORDER OF THE PURE PRO22(SLASH)LEU25 FORM OF CRAMBIN AT 150K REFINED TO 1.05 ANGSTROMS RESOLUTION

Released:
DOI: 10.2210/pdb1cnr/pdb
PDB entry 1cnr coloured by chain, front view.
PDB entry 1cnr coloured by chain, side view.
PDB entry 1cnr coloured by chain, top view.
Source organism: Crambe hispanica subsp. abyssinica
Primary publication:
Correlated disorder of the pure Pro22/Leu25 form of crambin at 150 K refined to 1.05-A resolution.
Yamano A, Teeter MM
J Biol Chem 269 13956-65 (1994)
PMID: 8188676

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-134358 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Crambin Chain: A
Molecule details ›
Chain: A
Length: 46 amino acids
Theoretical weight: 4.74 KDa
Source organism: Crambe hispanica subsp. abyssinica
Expression system: Not provided
UniProt:
  • Canonical: P01542 (Residues: 1-46; Coverage: 100%)
Gene name: THI2
Sequence domains: Plant thionin
Structure domains: Thionin-like

Ligands and Environments

1 bound ligand:
Ligand EOH 1 x EOH
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P21
Unit cell:
a: 40.621Å b: 18.345Å c: 22.14Å
α: 90° β: 91.03° γ: 90°
R-values:
R R work R free
0.105 not available not available
Expression system: Not provided

Quick links

Citations

2 review citations

Plant gamma-thionins: novel insights on the mechanism of action of a multi-functional class of defense proteins.
Pelegrini et al. (2005)
1 more

5 mentions without citation

Chemical shift prediction for protein structure calculation and quality assessment using an optimally parameterized force field.
Nielsen et al. (2012)
4 more