3AU0: Clumping factor B

Structural and biochemical characterization of ClfB:ligand interactions. Determined by X-ray diffraction at 2.45 Å resolution. Released 4 May 2011.

Method
X-ray diffraction
Resolution
2.45 Å
Organism
Staphylococcus aureus
Chains
1
Atoms
2,821
Mol. weight
37.46 kDa
Ligands
MG
Released
4 May 2011

Explore 3AU0 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3AU0 contains 7 α-helices and 29 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: 7 helices, 29 β-strands

ElementResiduesLengthSheet
β-strand21411
α-helix216-2183
β-strand219-22682
β-strand230-23123
α-helix233-2353
β-strand239-24792
β-strand25314
β-strand25514
β-strand256-26051
β-strand265-26625
β-strand27116
β-strand279-28681
β-strand292-29981
β-strand304-30961
α-helix311-3133
β-strand320-32782
β-strand328-32925
β-strand338-34143
β-strand344-34631
β-strand350-35121
β-strand354-35743
α-helix359-3613
β-strand374-38186
β-strand389-39686
β-strand403-41197
α-helix417-4193
β-strand422-42326
β-strand430-43676
α-helix439-4413
β-strand455-45736
α-helix460-4623
β-strand466-46727
β-strand473-48197
β-strand485-49396
β-strand500-509107
β-strand518-52697

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Clumping factor BAprotein339Staphylococcus aureusQ7A382 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>3AU0_1 Clumping factor B (chains A)
PVVNVADAKGTNVNDKVTASNFKLEKTTFDPNQSGNTFMAANFTVTDKVKSGDYFTAKLP
DSLTGNGDVDYSNSNNTMPIADIKSTNGDVVAKATYDILTKTYTFVFTDYVNNKENINGQ
FSLPLFTDRAKAPKSGTYDANINIADEMFNNKITYNYSSPIAGIDKPNGANISSQIIGVD
TASGQNTYKQTVFVNPKQRVLGNTWVYIKGYQDKIEESSGKVSATDTKLRIFEVNDTSKL
SESYYADPNDSNLKEVTDQFKNRIYYEHPNVASIKFGDITKTYVVLVEGHYDNTGKNLKT
QVIQENVDPVTNRDYSIFGWNNENVVRYGGGSADGDSAV

Ligands and cofactors

IDNameFormulaCopies
MGMagnesium ionMg2

Primary citation

Structural and biochemical characterization of ClfB:ligand interactions. Ganesh, V.K., Barbu, E.M., Deivanayagam, C.C.S. et al. To be published.

Other PDB entries of the same protein (UniProt Q7A382 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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