1Y6L: Human ubiquitin conjugating enzyme E2E2

Name: PDB 1Y6L: Human ubiquitin conjugating enzyme E2E2
Published: 2005-01-11
License: https://creativecommons.org/publicdomain/zero/1.0/
Keywords: ligase

Human ubiquitin conjugating enzyme E2E2. Determined by X-ray diffraction at 1.85 Å resolution. Released 11 Jan 2005.

Method: X-ray diffraction
Resolution: 1.85 Å
Organism: Homo sapiens
Chains: 3
Atoms: 3,855
Mol. weight: 49.84 kDa
Released: 11 Jan 2005

Explore 1Y6L in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1Y6L contains 24 α-helices and 23 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.

Chains A and B: 8 helices, 8 β-strands

Element	Residues	Length	Sheet
α-helix	1-15	15
α-helix	17-18	2
β-strand	21-25	5	1
β-strand	32-38	7	1
α-helix	39-40	2
β-strand	49-55	7	1
α-helix	64-65	2
β-strand	66-69	4	1
β-strand	75	1	2
β-strand	78	1	2
β-strand	83	1	1
β-strand	84	1	2
α-helix	87-89	3
α-helix	99-111	13
α-helix	121-129	9
α-helix	131-145	15

Chain C: 8 helices, 7 β-strands

Element	Residues	Length	Sheet
α-helix	1-15	15
α-helix	17-18	2
β-strand	21-25	5	5
β-strand	32-38	7	5
α-helix	39-40	2
β-strand	49-55	7	5
α-helix	64-65	2
β-strand	66-69	4	5
β-strand	78	1	6
β-strand	83	1	5
β-strand	84	1	6
α-helix	87-89	3
α-helix	99-111	13
α-helix	121-129	9
α-helix	131-145	15

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Ubiquitin-conjugating enzyme E2E2	A, B, C	protein	149	Homo sapiens	Q96LR5 (AlphaFold model)

Sequence of entity 1 (A, B, C), FASTA

>1Y6L_1 Ubiquitin-conjugating enzyme E2E2 (chains A, B, C)
GSTSAKRIQKELAEITLDPPPNCSAGPKGDNIYEWRSTILGPPGSVYEGGVFFLDITFSP
DYPFKPPKVTFRTRIYHCNINSQGVICLDILKDNWSPALTISKVLLSICSLLTDCNPADP
LVGSIATQYMTNRAEHDRMARQWTKRYAT

Primary citation

A human ubiquitin conjugating enzyme (E2)-HECT E3 ligase structure-function screen. Sheng, Y., Hong, J.H., Doherty, R. et al. Mol Cell Proteomics (2012) 11:329-341. DOI 10.1074/mcp.O111.013706 · PubMed

Other PDB entries of the same protein (UniProt Q96LR5 (AlphaFold model), which also has an AlphaFold model), best resolution first:

6W9A 2.3 Å, RNF12 RING domain in complex with Ube2e2
9BJZ 2.83 Å, Structure of the human DDD-Ube2e2 complex
9LTO 2.92 Å, Cryo-EM structure of DDB1-DDA1-DET1-Ube2e2 complex
9LTR 3.03 Å, Cryo-EM structure of dimeric DDB1-DDA1-DET1-Ube2e2-COP1 complex
9LTZ 3.26 Å, protein structure of DDB1-DDA1-DET1-Ube2e2 complex
9LU1 3.62 Å, protein structure of DDB1-DDA1-DET1-Ube2e2 bound to COP1 dimer
9W90 3.7 Å, DDB1-DDA1-DET1-Ube2e2-COP1-c-Jun-STK40 complex
9M0Y 4.25 Å, Local refinement of stacked like DDB1-DDA1-DET1-Ube2e2-COP1 complex (layer 2)
9LUL 4.99 Å, Local refinement of stacked like DDB1-DDA1-DET1-Ube2e2-COP1 complex (layer 1)

Browse structure collections

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