› 2m3t

Solution NMR

Solution-state NMR structure of wild-type human gamma(S)-crystallin

Released:
DOI: 10.2210/pdb2m3t/pdb
PDB entry 2m3t coloured by chain, ensemble of 21 models, front view.
PDB entry 2m3t coloured by chain, ensemble of 21 models, side view.
PDB entry 2m3t coloured by chain, ensemble of 21 models, top view.
Source organism: Homo sapiens
Primary publication:
Preferential and specific binding of human αB-crystallin to a cataract-related variant of γS-crystallin.
Kingsley CN, Brubaker WD, Markovic S, Diehl A, Brindley AJ, Oschkinat H, Martin RW
Structure 21 2221-7 (2013)
PMID: 24183572

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-149840 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Gamma-crystallin S Chain: A
Molecule details ›
Chain: A
Length: 178 amino acids
Theoretical weight: 20.96 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P22914 (Residues: 2-178; Coverage: 99%)
Gene names: CRYG8, CRYGS
Sequence domains: Beta/Gamma crystallin
Structure domains: Crystallins

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 87%
Refinement method: simulated annealing
Expression system: Escherichia coli

Quick links

Citations

5 review citations

Chaperones and chaperone-substrate complexes: Dynamic playgrounds for NMR spectroscopists.
Burmann et al. (2015)
4 more

19 mentions without citation

Functions of crystallins in and out of lens: roles in elongated and post-mitotic cells.
Slingsby et al. (2014)
18 more