5KTG: Mouse Bak BH3-in-groove homodimer

Crystal structure of mouse Bak BH3-in-groove homodimer (GFP). Determined by X-ray diffraction at 2.8 Å resolution. Released 17 Aug 2016.

Method
X-ray diffraction
Resolution
2.8 Å
Organisms
Aequorea victoria, Mus musculus
Chains
2
Atoms
4,910
Mol. weight
69.8 kDa
Released
17 Aug 2016

Explore 5KTG in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5KTG contains 21 α-helices and 28 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: 12 helices, 14 β-strands

ElementResiduesLengthSheet
α-helix4-96
β-strand12-22111
β-strand25-36121
β-strand41-4881
α-helix57-604
α-helix69-713
β-strand7311
α-helix741
α-helix76-816
α-helix83-875
β-strand92-10091
β-strand105-115111
β-strand118-128111
β-strand14112
β-strand148-15581
α-helix156-1583
β-strand160-170111
β-strand17112
β-strand176-187121
α-helix194-1974
β-strand199-208101
β-strand217-227111
α-helix1067-10704
α-helix1072-109827
α-helix1105-111713
α-helix1123-114220
Chain B: 9 helices, 14 β-strands
ElementResiduesLengthSheet
β-strand12-22113
β-strand25-36123
β-strand41-4773
α-helix57-604
α-helix69-713
β-strand7313
α-helix741
α-helix79-813
α-helix84-874
β-strand92-10093
β-strand105-115113
β-strand118-128113
β-strand14114
β-strand148-15583
β-strand160-170113
β-strand17114
β-strand176-187123
α-helix196-1972
β-strand199-208103
β-strand217-227113
α-helix231-109532
α-helix1102-111716
α-helix1123-114220

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Green fluorescent protein, Bcl-2 homologous antagonist/killerA, Bprotein309Aequorea victoria, Mus musculusO08734 (AlphaFold model), P42212 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>5KTG_1 Green fluorescent protein, Bcl-2 homologous antagonist/killer (chains A, B)
MSKGEELFTGVVPILVELDGDVNGHKFSVSGEGEGDATYGKLTLKFICTTGKLPVPWPTL
VTTFXVQCFARYPDHMKQHDFFKSAMPEGYVQERTIFFKDDGNYKTRAEVKFEGDTLVNR
IELKGIDFKEDGNILGHKLEYNYNSHNVYIMADKQKNGIKVNFKIRHNIEDGSVQLADHY
QQNTPIGDGPVLLPDNHYLSTQSNLSKDPNEKRDHMVLLEFVTAAGITGSNSILGQVGRQ
LALIGDDICRRYDTEFQNLLEQLQPTAGNAYELFTKIASSLFKSGISWGRVVALLGFGYR
LALYVYQRG

Primary citation

Assembly of Bak homodimers into higher order homooligomers in the mitochondrial apoptotic pore. Mandal, T., Shin, S., Aluvila, S. et al. Sci Rep (2016) 6:30763-30763. DOI 10.1038/srep30763 · PubMed

Other PDB entries of the same protein (UniProt O08734 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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