1MK3: Human bcl-W protein

Solution structure of human bcl-W protein. Determined by solution NMR. Released 3 Jun 2003.

Method: Solution NMR
Organism: Homo sapiens
Chains: 1
Atoms: 1,389
Mol. weight: 19.66 kDa
Released: 3 Jun 2003

Explore 1MK3 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1MK3 contains 9 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: 9 helices, 0 β-strands

Element	Residues	Length
α-helix	9-22	14
α-helix	41-55	15
α-helix	59-69	11
α-helix	75-86	12
α-helix	93-111	19
α-helix	115-131	17
α-helix	133-140	8
α-helix	143-147	5
α-helix	155-167	13

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Apoptosis regulator Bcl-W	A	protein	178	Homo sapiens	Q92843 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>1MK3_1 Apoptosis regulator Bcl-W (chains A)
ATPASAPDTRALVADFVGYKLRQKGYVCGAGPGEGPAADPLHQAMRAAGDEFETRFRRTF
SDLAAQLHVTPGSAQQRFTQVSDELFQGGPNWGRLVAFFVFGAALCAESVNKEMEVLVGQ
VQEWMVAYLETRLADWIHSSGGWAEFTALYGDGALEEARRLREGNWASVRLEHHHHHH

Primary citation

Solution structure of human BCL-w: modulation of ligand binding by the C-terminal helix. Denisov, A.Y., Madiraju, M.S., Chen, G. et al. J Biol Chem (2003) 278:21124-21128. DOI 10.1074/jbc.M301798200 · PubMed

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

4CIM 1.5 Å, Complex of a Bcl-w BH3 mutant with a BH3 domain
2Y6W 2.0 Å, Structure of a Bcl-w dimer
1O0L The structure of bcl-W reveals a role for the C-terminal residues in modulating…
1ZY3 Structural model of complex of Bcl-w protein with Bid BH3-peptide

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