1AB7: Barstar

NMR 15N relaxation and structural studies reveal conformational exchange in barstar C40/82A, 30 structures. Determined by solution NMR. Released 4 Sept 1997.

Method
Solution NMR
Organism
Bacillus amyloliquefaciens
Chains
1
Atoms
718
Mol. weight
10.16 kDa
Released
4 Sept 1997

Explore 1AB7 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1AB7 contains 4 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: 4 helices, 3 β-strands

ElementResiduesLengthSheet
β-strand2-541
α-helix13-208
α-helix21-255
α-helix34-418
β-strand49-5351
α-helix67-8014
β-strand84-8741

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
BarstarAprotein89Bacillus amyloliquefaciensP11540 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>1AB7_1 BARSTAR (chains A)
KKAVINGEQIRSISDLHQTLKKELALPEYYGENLDALWDALTGWVEYPLVLEWRQFEQSK
QLTENGAESVLQVFREAKAEGADITIILS

Primary citation

NMR 15N relaxation and structural studies reveal slow conformational exchange in barstar C40/82A. Wong, K.B., Fersht, A.R., Freund, S.M. J Mol Biol (1997) 268:494-511. DOI 10.1006/jmbi.1997.0989 · 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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