› 4fc1

Neutron Diffraction
1.1Å resolution

Ultra-high resolution neutron structure of crambin at room-temperature

Released:
DOI: 10.2210/pdb4fc1/pdb
PDB entry 4fc1 coloured by chain, front view.
PDB entry 4fc1 coloured by chain, side view.
PDB entry 4fc1 coloured by chain, top view.
Source organism: Crambe hispanica subsp. abyssinica
Primary publication:
Direct observation of hydrogen atom dynamics and interactions by ultrahigh resolution neutron protein crystallography.
Chen JC, Hanson BL, Fisher SZ, Langan P, Kovalevsky AY
Proc Natl Acad Sci U S A 109 15301-6 (2012)
PMID: 22949690

Function and Biology Details

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

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
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 DOD 42 x DOD
No modified residues

Experiments and Validation Details

Spacegroup: P21
Unit cell:
a: 22.795Å b: 18.826Å c: 41.042Å α: 90° β: 90.89° γ: 90°
R-values:
R R work R free 0.213 not available 0.253

Quick links

Citations

4 review citations

Carbon-oxygen hydrogen bonding in biological structure and function.
Horowitz et al. (2012)
3 more

8 mentions without citation

Fifteen years of the Protein Crystallography Station: the coming of age of macromolecular neutron crystallography.
Chen et al. (2017)
7 more