2BH8: Combinatorial Protein 1b11

Combinatorial Protein 1b11. Determined by X-ray diffraction at 1.9 Å resolution. Released 7 Feb 2005.

Method
X-ray diffraction
Resolution
1.9 Å
Organism
ESCHERICHIA COLI
Chains
2
Atoms
1,403
Mol. weight
21.48 kDa
Released
7 Feb 2005

Explore 2BH8 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2BH8 contains 6 α-helices and 12 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: 4 helices, 6 β-strands

ElementResiduesLengthSheet
β-strand19-2791
α-helix28-303
β-strand32-3761
β-strand43-4751
α-helix56-572
α-helix59-613
β-strand66-7381
β-strand77-8152
β-strand87-98122
α-helix99-1013
Chain B: 2 helices, 6 β-strands
ElementResiduesLengthSheet
β-strand17-27112
β-strand32-3762
β-strand43-4752
α-helix50-534
α-helix59-624
β-strand66-7382
β-strand77-8151
β-strand87-98121

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
1B11A, Bprotein101ESCHERICHIA COLIP0AG67 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>2BH8_1 1B11 (chains A, B)
MRGSHHHHGSRLQSGKMTGIVKWFNADKGFGFITPDDGSKDVFVHFSAGSSGAAVRGNPQ
QGDRVEGKIKSITDFGIFIGLDGGIDGLVHLSDISWAQAEA

Primary citation

A Segment of Cold Shock Protein Directs the Folding of a Combinatorial Protein. De Bono, S., Riechmann, L., Girard, E. et al. Proc Natl Acad Sci U S A (2005) 102:1396. DOI 10.1073/PNAS.0407298102 · PubMed

Other PDB entries of the same protein (UniProt P0AG67 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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