6NYD: S. cerevisiae Ubc3

Crystal Structure of S. cerevisiae Ubc3 (Cdc34). Determined by X-ray diffraction at 1.65 Å resolution. Released 7 Aug 2019.

Method
X-ray diffraction
Resolution
1.65 Å
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Chains
1
Atoms
1,515
Mol. weight
22.87 kDa
Ligands
ZN
Released
7 Aug 2019

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

Secondary structure: helices and β-sheets

6NYD contains 7 α-helices and 7 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 C: 7 helices, 7 β-strands

ElementResiduesLengthSheet
α-helix4-2017
β-strand29-3461
β-strand38-4691
β-strand60-6561
β-strand76-7941
β-strand8812
β-strand9311
β-strand9412
α-helix97-993
α-helix121-13313
α-helix143-1519
α-helix153-16715
α-helix168-1703
α-helix1721

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Ubiquitin-conjugating enzyme E2-34 kDaCprotein197Saccharomyces cerevisiae (strain ATCC 204508 / S288c)P14682 (AlphaFold model)
Sequence of entity 1 (C), FASTA
>6NYD_1 Ubiquitin-conjugating enzyme E2-34 kDa (chains C)
GAMASRKSTASSLLLRQYRELTDPKKAIPSFHIELEDDSNIFTWNIGVMVLNEDSIYHGG
FFKAQMRFPEDFPFSPPQFRFTPAIYHPNVYRDGRLCISILHQSGDPMTDEPDAETWSPV
QTVESVLISIVSLLEDPNINSPANVDAAVDYRKNPEQYKQRVKMEVERSKQDIPKGFIMP
TSESAYISQSKLDEPES

Ligands and cofactors

IDNameFormulaCopies
ZNZinc ionZn4

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

Primary citation

Structural insights into E1 recognition and the ubiquitin-conjugating activity of the E2 enzyme Cdc34. Williams, K.M., Qie, S., Atkison, J.H. et al. Nat Commun (2019) 10:3296-3296. DOI 10.1038/s41467-019-11061-8 · PubMed

Other PDB entries of the same protein (UniProt P14682 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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