1B0W: Bence-jones kappa I protein bre

Structural comparison of amyloidogenic light chain dimer in two crystal forms with nonamyloidogenic counterparts. Determined by X-ray diffraction at 1.8 Å resolution. Released 16 Nov 1998.

Method
X-ray diffraction
Resolution
1.8 Å
Organism
Homo sapiens
Chains
3
Atoms
2,624
Mol. weight
35.84 kDa
Released
16 Nov 1998

Explore 1B0W in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1B0W contains 9 α-helices and 33 β-strands across 3 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.

Chain A: 3 helices, 11 β-strands

ElementResiduesLengthSheet
β-strand4-741
β-strand10-1342
β-strand19-2571
β-strand33-3862
β-strand45-4952
β-strand53-5422
α-helix551
β-strand62-6761
β-strand70-7561
α-helix80-823
β-strand84-9072
α-helix961
β-strand9812
β-strand102-10652
Chains B and C: 3 helices, 11 β-strands
ElementResiduesLengthSheet
β-strand4-743
β-strand10-1344
β-strand19-2573
β-strand33-3864
β-strand45-4954
β-strand53-5424
α-helix551
β-strand62-6763
β-strand70-7563
α-helix80-823
β-strand84-9074
α-helix961
β-strand97-9824
β-strand102-10654

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Bence-jones kappa I protein breA, B, Cprotein108Homo sapiensP01594 (AlphaFold model)
Sequence of entity 1 (A, B, C), FASTA
>1B0W_1 BENCE-JONES KAPPA I PROTEIN BRE (chains A, B, C)
DIQMTQSPSSLSASVGDRVTITCQASQDISDYLIWYQQKLGKAPNLLIYDASTLETGVPS
RFSGSGSGTEYTFTISSLQPEDIATYYCQQYDDLPYTFGQGTKVEIKR

Primary citation

Tertiary structures of amyloidogenic and non-amyloidogenic transthyretin variants: new model for amyloid fibril formation. Schormann, N., Murrell, J.R., Benson, M.D. Amyloid (1998) 5:175-187. PubMed

Other PDB entries of the same protein (UniProt P01594 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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