9LAF: Elongin BC-EPOP peptide

Crystal structure of Elongin BC-EPOP peptide. Determined by X-ray diffraction at 2.14 Å resolution. Released 21 May 2025.

Method
X-ray diffraction
Resolution
2.14 Å
Organism
Homo sapiens
Chains
3
Atoms
1,644
Mol. weight
25.55 kDa
Released
21 May 2025

Explore 9LAF in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

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.

Chain A: 2 helices, 0 β-strands

ElementResiduesLengthSheet
α-helix37-393
α-helix40-4910
Chain B: 7 helices, 11 β-strands
ElementResiduesLengthSheet
β-strand2-981
β-strand1012
β-strand12-1981
β-strand2313
α-helix24-3512
α-helix39-413
β-strand42-4651
β-strand49-5021
α-helix51-522
β-strand5613
α-helix57-604
β-strand6814
β-strand7114
α-helix721
β-strand73-7971
α-helix86-883
β-strand9012
α-helix91-933
Chain C: 5 helices, 3 β-strands
ElementResiduesLengthSheet
β-strand18-2251
β-strand28-3251
α-helix33-364
α-helix40-456
β-strand59-6131
α-helix67-8317
α-helix97-993
α-helix100-11011

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Elongin-BBprotein104Homo sapiensQ15370 (AlphaFold model)
Elongin-CCprotein96Homo sapiensQ15369 (AlphaFold model)
Elongin BC and Polycomb repressive complex 2-associated proteinAprotein26Homo sapiensA6NHQ4 (AlphaFold model)
Sequence of entity 1 (B), FASTA
>9LAF_1 Elongin-B (chains B)
MDVFLMIRRHKTTIFTDAKESSTVFELKRIVEGILKRPPDEQRLYKDDQLLDDGKTLGEC
GFTSQTARPQAPATVGLAFRADDTFEALCIEPFSSPPELPDVMK
Sequence of entity 2 (C), FASTA
>9LAF_2 Elongin-C (chains C)
MYVKLISSDGHEFIVKREHALTSGTIKAMLSGPGQFAENETNEVNFREIPSHVLSKVCMY
FTYKVRYTNSSTEIPEFPIAPEIALELLMAANFLDC
Sequence of entity 3 (A), FASTA
>9LAF_3 Elongin BC and Polycomb repressive complex 2-associated protein (chains A)
MHHHHHHGSEFSPLCLRALAFCALAK

Primary citation

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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