2N0K: Alpha-crystallin B chain

Chemical shift assignments and structure of the alpha-crystallin domain from human, HSPB5. Determined by solution NMR. Released 3 Jun 2015.

Method
Solution NMR
Organism
Homo sapiens
Chains
2
Atoms
1,436
Mol. weight
20.4 kDa
Released
3 Jun 2015

Explore 2N0K in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2N0K contains 4 α-helices and 30 β-strands across 2 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chains A and B: 2 helices, 15 β-strands

ElementResiduesLengthSheet
β-strand68-7141
β-strand74-7741
β-strand78-8032
β-strand90-9343
β-strand97-10153
β-strand103-10864
β-strand113-11754
β-strand120-12343
α-helix124-1252
β-strand12815
α-helix130-1323
β-strand13416
β-strand13712
β-strand142-14432
β-strand14616
β-strand147-14821
β-strand14915

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Alpha-crystallin B chainA, Bprotein89Homo sapiensP02511 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>2N0K_1 Alpha-crystallin B chain (chains A, B)
GLSEMRLEKDRFSVNLDVKHFSPEELKVKVLGDVIEVHGKHEERQDEHGFISREFHRKYR
IPADVDPLTITSSLSSDGVLTVDGPRKQV

Primary citation

A conserved histidine modulates HSPB5 structure to trigger chaperone activity in response to stress-related acidosis. Rajagopal, P., Tse, E., Borst, A.J. et al. Elife (2015) 4. DOI 10.7554/eLife.07304 · PubMed

Other PDB entries of the same protein (UniProt P02511 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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