› 1e7n

X-ray diffraction
2.35Å resolution

The N-terminal domain of beta-B2-crystallin resembles the putative ancestral homodimer

Released:
DOI: 10.2210/pdb1e7n/pdb
PDB entry 1e7n coloured by chain, front view.
PDB entry 1e7n coloured by chain, side view.
PDB entry 1e7n coloured by chain, top view.
Source organism: Mus musculus
Primary publication:
The N-terminal domain of betaB2-crystallin resembles the putative ancestral homodimer.
Clout NJ, Basak A, Wieligmann K, Bateman OA, Jaenicke R, Slingsby C
J Mol Biol 304 253-7 (2000)
PMID: 11090271

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-158663 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Beta-crystallin B2 Chains: A, B
Molecule details ›
Chains: A, B
Length: 106 amino acids
Theoretical weight: 11.91 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
  • Canonical: P62696 (Residues: 2-107; Coverage: 52%)
Gene name: Crybb2
Sequence domains: Beta/Gamma crystallin
Structure domains: Crystallins

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY
Spacegroup: P65
Unit cell:
a: 110.96Å b: 110.96Å c: 29.88Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.212 0.212 0.246
Expression system: Escherichia coli

Quick links

Citations

5 review citations

Ageing and vision: structure, stability and function of lens crystallins.
Bloemendal et al. (2004)
4 more

3 mentions without citation

Evolution of crystallins for a role in the vertebrate eye lens.
Slingsby et al. (2013)
2 more