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.
Explore 3FSH in 3D Show helices and sheets RCSB PDB PDBe
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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 0-18 | 19 | |
| β-strand | 24-28 | 5 | 1 |
| β-strand | 36-42 | 7 | 1 |
| α-helix | 43-44 | 2 | |
| β-strand | 53-59 | 7 | 1 |
| β-strand | 70-73 | 4 | 1 |
| β-strand | 82 | 1 | 2 |
| β-strand | 87 | 1 | 1 |
| β-strand | 88 | 1 | 2 |
| α-helix | 91-93 | 3 | |
| α-helix | 116-128 | 13 | |
| α-helix | 132-134 | 3 | |
| α-helix | 138-145 | 8 | |
| α-helix | 148-162 | 15 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 0-18 | 19 | |
| α-helix | 20-21 | 2 | |
| β-strand | 24-28 | 5 | 3 |
| β-strand | 36-42 | 7 | 3 |
| α-helix | 43-44 | 2 | |
| β-strand | 53-59 | 7 | 3 |
| β-strand | 70-73 | 4 | 3 |
| β-strand | 82 | 1 | 4 |
| β-strand | 87 | 1 | 3 |
| β-strand | 88 | 1 | 4 |
| α-helix | 91-93 | 3 | |
| α-helix | 116-126 | 11 | |
| α-helix | 138-145 | 8 | |
| α-helix | 148-163 | 16 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 582-597 | 16 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Ubiquitin-conjugating enzyme E2 G2 | A, B | protein | 168 | Mus musculus | P60605 (AlphaFold model) |
| Autocrine motility factor receptor, isoform 2 | C | protein | 28 | Q9UKV5 (AlphaFold model) |
>3FSH_1 Ubiquitin-conjugating enzyme E2 G2 (chains A, B) GSHMAGTALKRLMAEYKQLTLNPPEGIVAGPMNEENFFEWEALIMGPEDTCFEFGVFPAI LSFPLDYPLSPPKMRFTCEMFHPNIYPDGRVCISILHAPGDDPMGYESSAERWSPVQSVE KILLSVVSMLAEPNDESGANVDASKMWRDDREQFYKIAKQIVQKSLGL
>3FSH_2 Autocrine motility factor receptor, isoform 2 (chains C) SADERQRMLVQRKDELLQQARKRFLNKS
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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