6K3M: SpA IgG-binding domain protein,Protein A

Application of anti-helix antibodies in protein structure determination (8189-3LRH). Determined by X-ray diffraction at 1.8 Å resolution. Released 14 Aug 2019.

Method
X-ray diffraction
Resolution
1.8 Å
Organisms
Staphylococcus aureus, Homo sapiens
Chains
2
Atoms
1,449
Mol. weight
23.51 kDa
Released
14 Aug 2019

Explore 6K3M in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6K3M contains 6 α-helices and 11 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: 2 helices, 11 β-strands

ElementResiduesLengthSheet
β-strand5-621
β-strand9-1242
β-strand18-2361
β-strand35-3952
β-strand46-5052
β-strand54-5522
α-helix561
β-strand63-6861
β-strand71-7661
α-helix81-833
β-strand85-9392
β-strand98-10142
β-strand105-10952
Chain H: 4 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix5-1612
α-helix22-3413
α-helix36-383
α-helix39-6224

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
SpA IgG-binding domain protein,Protein AHprotein82Staphylococcus aureusP02976 (AlphaFold model)
3LRH intrabodyAprotein135Homo sapiens
Sequence of entity 1 (H), FASTA
>6K3M_1 SpA IgG-binding domain protein,Protein A (chains H)
MGSSHHHHHHSSGLVPRGSHMFNKDQQSAFYEILNMPNLNEAQRNGFIQSLKDDPSQSTN
VLGEAKKLNKLQKAFESLKSFQ
Sequence of entity 2 (A), FASTA
>6K3M_2 3LRH intrabody (chains A)
MGSSHHHHHHSSGLVPRGSHMGSQPVLTQSPSVSAAPRQRVTISVSGSNSNIGSNTVNWI
QQLPGRAPELLMYDDDLLAPGVSDRFSGSRSGTSASLTISGLQSEDEADYYAATWDDSLN
GWVFGGGTKVTVLSA

Primary citation

Application of antihelix antibodies in protein structure determination. Kim, J.W., Kim, S., Lee, H. et al. Proc Natl Acad Sci U S A (2019) 116:17786-17791. DOI 10.1073/pnas.1910080116 · PubMed

Other PDB entries of the same protein (UniProt P02976 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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