› 1blb

X-ray diffraction
3.3Å resolution

CLOSE PACKING OF AN OLIGOMERIC EYE LENS BETA-CRYSTALLIN INDUCES LOSS OF SYMMETRY AND ORDERING OF SEQUENCE EXTENSIONS

Released:
DOI: 10.2210/pdb1blb/pdb
PDB entry 1blb coloured by chain, front view.
PDB entry 1blb coloured by chain, side view.
PDB entry 1blb coloured by chain, top view.
Source organism: Bos taurus
Primary publication:
Close packing of an oligomeric eye lens beta-crystallin induces loss of symmetry and ordering of sequence extensions.
Nalini V, Bax B, Driessen H, Moss DS, Lindley PF, Slingsby C
J Mol Biol 236 1250-8 (1994)
PMID: 8120900

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-135882 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Beta-crystallin B2 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 204 amino acids
Theoretical weight: 23.2 KDa
Source organism: Bos taurus
Expression system: Not provided
UniProt:
  • Canonical: P02522 (Residues: 2-205; Coverage: 100%)
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
Spacegroup: C222
Unit cell:
a: 154.71Å b: 165.9Å c: 78.48Å
α: 90° β: 90° γ: 90°
Expression system: Not provided

Quick links

Citations

3 review citations

Lens β-crystallins: the role of deamidation and related modifications in aging and cataract.
Lampi et al. (2014)
2 more

15 mentions without citation

Protein acrobatics in pairs--dimerization via domain swapping.
Gronenborn AM. (2009)
14 more