4KGR: PDB entry 4KGR

Backbone Modifications in the Protein GB1 Helix: beta-3-Ala24, beta-3-Lys28, beta-3-Lys31, beta-3-Asn35. Determined by X-ray diffraction at 2.0 Å resolution. Released 4 Sept 2013.

Method
X-ray diffraction
Resolution
2.0 Å
Chains
8
Atoms
3,731
Mol. weight
49.99 kDa
Released
4 Sept 2013

Explore 4KGR in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4KGR contains 13 α-helices and 32 β-strands across 8 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.

Chains A, B and H: 1 helix, 4 β-strands

ElementResiduesLengthSheet
β-strand2-871
β-strand13-1971
α-helix23-3614
β-strand42-4651
β-strand51-5551
Chains C, D, E, F and G: 2 helices, 4 β-strands
ElementResiduesLengthSheet
β-strand2-872
β-strand13-1972
α-helix23-3614
β-strand42-4652
α-helix47-493
β-strand51-5552

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Streptococcal Protein GB1 Backbone Modified Variant: beta-3-Ala24, beta-3-Lys28, beta-3-Lys31,…A, B, C, D, E, F, G, Hprotein57P06654 (AlphaFold model)
Sequence of entity 1 (A, B, C, D, E, F, G, H), FASTA
>4KGR_1 Streptococcal Protein GB1 Backbone Modified Variant: beta-3-Ala24, beta-3-Lys28, beta-3-Lys31, beta-3-Asn35 (chains A, B, C, D, E, F, G, H)
DTYKLILNGKTLKGETTTEAVDAATAEKVFKQYANDNGVDGEWTYDDATKTFTVTEX

Primary citation

Protein-like Tertiary Folding Behavior from Heterogeneous Backbones. Reinert, Z.E., Lengyel, G.A., Horne, W.S. J Am Chem Soc (2013) 135:12528-12531. DOI 10.1021/ja405422v · PubMed

Other PDB entries of the same protein (UniProt P06654 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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