1BTB: Barstar

Three-dimensional solution structure and 13C assignments of barstar using nuclear magnetic resonance spectroscopy. Determined by solution NMR. Released 31 Jul 1994.

Method
Solution NMR
Organism
Bacillus amyloliquefaciens
Chains
1
Atoms
720
Mol. weight
10.22 kDa
Released
31 Jul 1994

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

Secondary structure: helices and β-sheets

1BTB contains 5 α-helices and 3 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: 5 helices, 3 β-strands

ElementResiduesLengthSheet
β-strand2-651
α-helix13-208
α-helix21-255
α-helix34-418
β-strand49-5461
α-helix58-614
α-helix67-7913
β-strand84-8851

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
BarstarAprotein89Bacillus amyloliquefaciensP11540 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>1BTB_1 BARSTAR (chains A)
KKAVINGEQIRSISDLHQTLKKELALPEYYGENLDALWDCLTGWVEYPLVLEWRQFEQSK
QLTENGAESVLQVFREAKAEGCDITIILS

Primary citation

Three-dimensional solution structure and 13C assignments of barstar using nuclear magnetic resonance spectroscopy. Lubienski, M.J., Bycroft, M., Freund, S.M. et al. Biochemistry (1994) 33:8866-8877. DOI 10.1021/bi00196a003 · PubMed

Other PDB entries of the same protein (UniProt P11540 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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