Crystal structure of Elongin BC-EPOP peptide. Determined by X-ray diffraction at 2.14 Å resolution. Released 21 May 2025.
Explore 9LAF in 3D Show helices and sheets RCSB PDB PDBe
9LAF contains 14 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 | 37-39 | 3 | |
| α-helix | 40-49 | 10 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 2-9 | 8 | 1 |
| β-strand | 10 | 1 | 2 |
| β-strand | 12-19 | 8 | 1 |
| β-strand | 23 | 1 | 3 |
| α-helix | 24-35 | 12 | |
| α-helix | 39-41 | 3 | |
| β-strand | 42-46 | 5 | 1 |
| β-strand | 49-50 | 2 | 1 |
| α-helix | 51-52 | 2 | |
| β-strand | 56 | 1 | 3 |
| α-helix | 57-60 | 4 | |
| β-strand | 68 | 1 | 4 |
| β-strand | 71 | 1 | 4 |
| α-helix | 72 | 1 | |
| β-strand | 73-79 | 7 | 1 |
| α-helix | 86-88 | 3 | |
| β-strand | 90 | 1 | 2 |
| α-helix | 91-93 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 18-22 | 5 | 1 |
| β-strand | 28-32 | 5 | 1 |
| α-helix | 33-36 | 4 | |
| α-helix | 40-45 | 6 | |
| β-strand | 59-61 | 3 | 1 |
| α-helix | 67-83 | 17 | |
| α-helix | 97-99 | 3 | |
| α-helix | 100-110 | 11 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Elongin-B | B | protein | 104 | Homo sapiens | Q15370 (AlphaFold model) |
| Elongin-C | C | protein | 96 | Homo sapiens | Q15369 (AlphaFold model) |
| Elongin BC and Polycomb repressive complex 2-associated protein | A | protein | 26 | Homo sapiens | A6NHQ4 (AlphaFold model) |
>9LAF_1 Elongin-B (chains B) MDVFLMIRRHKTTIFTDAKESSTVFELKRIVEGILKRPPDEQRLYKDDQLLDDGKTLGEC GFTSQTARPQAPATVGLAFRADDTFEALCIEPFSSPPELPDVMK
>9LAF_2 Elongin-C (chains C) MYVKLISSDGHEFIVKREHALTSGTIKAMLSGPGQFAENETNEVNFREIPSHVLSKVCMY FTYKVRYTNSSTEIPEFPIAPEIALELLMAANFLDC
>9LAF_3 Elongin BC and Polycomb repressive complex 2-associated protein (chains A) MHHHHHHGSEFSPLCLRALAFCALAK
Structural analysis of EPOP BC-box binding to the elongin BC complex. Kim, S., Yeo, H., Lee, B.I. Biochem Biophys Res Commun (2025) 759:151691-151691. DOI 10.1016/j.bbrc.2025.151691 · PubMed
Other PDB entries of the same protein (UniProt Q15370 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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