1O0L: Apoptosis regulator Bcl-W

The structure of bcl-W reveals a role for the C-terminal residues in modulating biological activity. Determined by solution NMR. Released 1 Apr 2003.

Method
Solution NMR
Organism
Homo sapiens
Chains
1
Atoms
1,428
Mol. weight
20.25 kDa
Released
1 Apr 2003

Explore 1O0L in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1O0L contains 11 α-helices and 0 β-strands across 1 chain. 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: 11 helices, 0 β-strands

ElementResiduesLengthSheet
α-helix10-2415
α-helix33-353
α-helix43-5614
α-helix61-677
α-helix76-8611
α-helix93-11119
α-helix116-12914
α-helix130-1345
α-helix135-1417
α-helix144-1507
α-helix157-17014

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Apoptosis regulator Bcl-WAprotein188Homo sapiensQ92843 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>1O0L_1 Apoptosis regulator Bcl-W (chains A)
GPLGSMATPASAPDTRALVADFVGYKLRQKGYVCGAGPGEGPAADPLHQAMRAAGDEFET
RFRRTFSDLAAQLHVTPGSAQQRFTQVSDELFQGGPNWGRLVAFFVFGAALCAESVNKEM
EPLVGQVQEWMVEYLETRLADWIHSSGGWAEFTALYGDGALEEARRLREGNWASVRTVLT
GAVALGAL

Primary citation

The structure of Bcl-w reveals a role for the C-terminal residues in modulating biological activity. Hinds, M.G., Lackmann, M., Skea, G.L. et al. EMBO J (2003) 22:1497-1507. DOI 10.1093/emboj/cdg144 · PubMed

Other PDB entries of the same protein (UniProt Q92843 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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