2ONQ: Immunoglobulin G-binding protein G

Gbeta1 stabilization by in vitro evolution and computational design. Determined by X-ray diffraction at 1.7 Å resolution. Released 8 Jan 2008.

Method
X-ray diffraction
Resolution
1.7 Å
Organism
Streptococcus sp.
Chains
1
Atoms
480
Mol. weight
6.33 kDa
Released
8 Jan 2008

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

Secondary structure: helices and β-sheets

2ONQ contains 1 α-helix and 4 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: 1 helix, 4 β-strands

ElementResiduesLengthSheet
β-strand2-871
β-strand13-1971
α-helix23-3614
β-strand42-4651
β-strand51-5551

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Immunoglobulin G-binding protein GAprotein56Streptococcus sp.P19909 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>2ONQ_1 Immunoglobulin G-binding protein G (chains A)
MQFKLIINGKTLKGEITIEAVDAAEAEKFFKQYANDNGIDGEWTYDDATKTFTVTE

Primary citation

Optimization of the gbeta1 domain by computational design and by in vitro evolution: structural and energetic basis of stabilization. Wunderlich, M., Max, K.E., Roske, Y. et al. J Mol Biol (2007) 373:775-784. DOI 10.1016/j.jmb.2007.08.004 · PubMed

Other PDB entries of the same protein (UniProt P19909 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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