2ESK: Ubiquitin-conjugating enzyme E2 D2

Human Ubiquitin-Conjugating Enzyme (E2) UbcH5b, wild-type. Determined by X-ray diffraction at 1.36 Å resolution. Released 6 Dec 2005.

Method
X-ray diffraction
Resolution
1.36 Å
Organism
Homo sapiens
Chains
1
Atoms
1,441
Mol. weight
16.88 kDa
Released
6 Dec 2005

Explore 2ESK in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2ESK 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 A: 7 helices, 7 β-strands

ElementResiduesLengthSheet
α-helix0-1516
β-strand21-2661
β-strand29-38101
α-helix39-402
β-strand49-5571
α-helix64-652
β-strand66-6941
β-strand7812
β-strand8311
β-strand8412
α-helix87-893
α-helix99-11113
α-helix121-1299
α-helix131-14515

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Ubiquitin-conjugating enzyme E2 D2Aprotein149Homo sapiensP62837 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>2ESK_1 Ubiquitin-conjugating enzyme E2 D2 (chains A)
GAMALKRIHKELNDLARDPPAQCSAGPVGDDMFHWQATIMGPNDSPYQGGVFFLTIHFPT
DYPFKPPKVAFTTRIYHPNINSNGSICLDILRSQWSPALTISKVLLSICSLLCDPNPDDP
LVPEIARIYKTDREKYNRIAREWTQKYAM

Primary citation

Mechanistic insight into the allosteric activation of a ubiquitin-conjugating enzyme by RING-type ubiquitin ligases. Ozkan, E., Yu, H., Deisenhofer, J. Proc Natl Acad Sci U S A (2005) 102:18890-18895. DOI 10.1073/pnas.0509418102 · PubMed

Other PDB entries of the same protein (UniProt P62837 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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