2M5B: BID-BAK complex

The NMR structure of the BID-BAK complex. Determined by solution NMR. Released 17 Apr 2013.

Method
Solution NMR
Organisms
Homo sapiens, Synthetic construct
Chains
2
Atoms
1,515
Mol. weight
21.48 kDa
Released
17 Apr 2013

Explore 2M5B in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2M5B contains 10 α-helices and 0 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.

Chain A: 8 helices, 0 β-strands

ElementResiduesLengthSheet
α-helix24-4926
α-helix70-8112
α-helix83-9715
α-helix107-11812
α-helix125-14521
α-helix151-16212
α-helix167-1737
α-helix177-1826
Chain B: 2 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix81-888
α-helix95-995

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Bcl-2 homologous antagonist/killerAprotein169Homo sapiensQ16611 (AlphaFold model)
human_BID_BH3_SAHBBprotein23Synthetic constructP55957 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>2M5B_1 Bcl-2 homologous antagonist/killer (chains A)
ALPSASEEQVAQDTEEVFRSYVFYRHQQEQEAEGVAAPADPEMVTLPLQPSSTMGQVGRQ
LAIIGDDINRRYDSEFQTMLQHLQPTAENAYEYFTKIATSLFESGINWGRVVALLGFGYR
LALHVYQHGLTGFLGQVTRFVVDFMLHHCIARWIAQRGGWVAALNLGNG
Sequence of entity 2 (B), FASTA
>2M5B_2 human_BID_BH3_SAHB (chains B)
EDIIRNIARHLALVGDLLDRSIX

Primary citation

BID-induced structural changes in BAK promote apoptosis. Moldoveanu, T., Grace, C.R., Llambi, F. et al. Nat Struct Mol Biol (2013) 20:589-597. DOI 10.1038/nsmb.2563 · PubMed

Other PDB entries of the same protein (UniProt Q16611 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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