1ZUK: Yeast BBC1 Sh3 domain

Yeast BBC1 Sh3 domain complexed with a peptide from Las17. Determined by X-ray diffraction at 1.9 Å resolution. Released 15 Aug 2006.

Method
X-ray diffraction
Resolution
1.9 Å
Organism
Saccharomyces cerevisiae
Chains
3
Atoms
1,354
Mol. weight
16.91 kDa
Ligands
MG
Released
15 Aug 2006

Explore 1ZUK in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1ZUK contains 5 α-helices and 16 β-strands across 3 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, 8 β-strands

ElementResiduesLengthSheet
α-helix4-52
β-strand8-1251
β-strand1612
β-strand2311
β-strand2612
β-strand31-3771
β-strand42-4871
β-strand54-6071
α-helix61-633
β-strand64-6631
Chain B: 2 helices, 8 β-strands
ElementResiduesLengthSheet
α-helix41
β-strand8-1253
β-strand1614
β-strand2313
β-strand2614
β-strand31-3773
β-strand42-4873
β-strand54-6073
α-helix61-633
β-strand64-6633
Chain C: 1 helix, 0 β-strands
ElementResiduesLengthSheet
α-helix3-108

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Myosin tail region-interacting protein MTI1A, Bprotein68Saccharomyces cerevisiaeP47068 (AlphaFold model)
Proline-rich protein LAS17Cprotein11Q12446 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>1ZUK_1 Myosin tail region-interacting protein MTI1 (chains A, B)
MSEPEVPFKVVAQFPYKSDYEDDLNFEKDQEIIVTSVEDAEWYFGEYQDSNGDVIEGIFP
KSFVAVQG
Sequence of entity 2 (C), FASTA
>1ZUK_2 Proline-rich protein LAS17 (chains C)
RGPAPPPPPHR

Ligands and cofactors

IDNameFormulaCopies
MGMagnesium ionMg2

Water and common crystallization additives (CL) are not listed.

Primary citation

Structural genomics of yeast SH3 domains. Kursula, P., Kursula, I., Lehmann, F. et al. To be published.

Other PDB entries of the same protein (UniProt P47068 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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