3FSH: Ubiquitin conjugating enzyme Ube2g2

Crystal structure of the ubiquitin conjugating enzyme Ube2g2 bound to the G2BR domain of ubiquitin ligase gp78. Determined by X-ray diffraction at 2.76 Å resolution. Released 10 Feb 2009.

Method
X-ray diffraction
Resolution
2.76 Å
Organism
Mus musculus
Chains
3
Atoms
2,862
Mol. weight
41.18 kDa
Released
10 Feb 2009

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

Secondary structure: helices and β-sheets

3FSH contains 15 α-helices and 14 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: 7 helices, 7 β-strands

ElementResiduesLengthSheet
α-helix0-1819
β-strand24-2851
β-strand36-4271
α-helix43-442
β-strand53-5971
β-strand70-7341
β-strand8212
β-strand8711
β-strand8812
α-helix91-933
α-helix116-12813
α-helix132-1343
α-helix138-1458
α-helix148-16215
Chain B: 7 helices, 7 β-strands
ElementResiduesLengthSheet
α-helix0-1819
α-helix20-212
β-strand24-2853
β-strand36-4273
α-helix43-442
β-strand53-5973
β-strand70-7343
β-strand8214
β-strand8713
β-strand8814
α-helix91-933
α-helix116-12611
α-helix138-1458
α-helix148-16316
Chain C: 1 helix, 0 β-strands
ElementResiduesLengthSheet
α-helix582-59716

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Ubiquitin-conjugating enzyme E2 G2A, Bprotein168Mus musculusP60605 (AlphaFold model)
Autocrine motility factor receptor, isoform 2Cprotein28Q9UKV5 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>3FSH_1 Ubiquitin-conjugating enzyme E2 G2 (chains A, B)
GSHMAGTALKRLMAEYKQLTLNPPEGIVAGPMNEENFFEWEALIMGPEDTCFEFGVFPAI
LSFPLDYPLSPPKMRFTCEMFHPNIYPDGRVCISILHAPGDDPMGYESSAERWSPVQSVE
KILLSVVSMLAEPNDESGANVDASKMWRDDREQFYKIAKQIVQKSLGL
Sequence of entity 2 (C), FASTA
>3FSH_2 Autocrine motility factor receptor, isoform 2 (chains C)
SADERQRMLVQRKDELLQQARKRFLNKS

Primary citation

Mechanistic insights into active site-associated polyubiquitination by the ubiquitin-conjugating enzyme Ube2g2. Li, W., Tu, D., Li, L. et al. Proc Natl Acad Sci U S A (2009) 106:3722-3727. DOI 10.1073/pnas.0808564106 · PubMed

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