8EI2: N-terminal domain of CUL5

Crystal structure of the N-terminal domain of CUL5 in complex with H314, a Helicon Polypeptide. Determined by X-ray diffraction at 2.8 Å resolution. Released 25 Oct 2023.

Method
X-ray diffraction
Resolution
2.8 Å
Organisms
Homo sapiens, synthetic construct
Chains
2
Atoms
3,067
Mol. weight
47.04 kDa
Ligands
WHL
Released
25 Oct 2023

Explore 8EI2 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

8EI2 contains 25 α-helices and 0 β-strands across 2 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: 24 helices, 0 β-strands

ElementResiduesLengthSheet
α-helix15-3016
α-helix37-5317
α-helix58-8023
α-helix88-10316
α-helix114-1174
α-helix134-14310
α-helix144-1485
α-helix149-16618
α-helix175-18713
α-helix198-2025
α-helix203-21513
α-helix218-2247
α-helix227-24317
α-helix245-2484
α-helix258-26912
α-helix271-2733
α-helix274-2785
α-helix281-2866
α-helix290-30011
α-helix308-32417
α-helix337-3404
α-helix343-35917
α-helix363-3719
α-helix374-3763
Chain C: 1 helix, 0 β-strands
ElementResiduesLengthSheet
α-helix4-1512

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Cullin-5Aprotein387Homo sapiensQ93034 (AlphaFold model)
H314Cprotein18synthetic construct
Sequence of entity 1 (A), FASTA
>8EI2_1 Cullin-5 (chains A)
SMATSNLLKNKGSLQFEDKWDFMRPIVLKLLRQESVTKQQWFDLFSDVHAVCLWDDKGPA
KIHQALKEDILEFIKQAQARVLSHQDDTALLKAYIVEWRKFFTQCDILPKPFCQLEITLM
GKQGSNKKSNVEDSIVRKLMLDTWNESIFSNIKNRLQDSAMKLVHAERLGEAFDSQLVIG
VRESYVNLCSNPEDKLQIYRDNFEKAYLDSTERFYRTQAPSYLQQNGVQNYMKYADAKLK
EEEKRALRYLETRRECNSVEALMECCVNALVTSFKETILAECQGMIKRNETEKLHLMFSL
MDKVPNGIEPMLKDLEEHIISAGLADMVAAAETITTDSEKYREQLDTLFNRFSKLVKEAF
QDDPRFLTARDKAYKAVVNDATIFKLE
Sequence of entity 2 (C), FASTA
>8EI2_2 H314 (chains C)
XDPAWYDCADAAWICTFX

Ligands and cofactors

IDNameFormulaCopies
WHLN,N'-(1,4-phenylene)diacetamideC10 H12 N2 O21

Primary citation

Recognition and reprogramming of E3 ubiquitin ligase surfaces by alpha-helical peptides. Tokareva, O.S., Li, K., Travaline, T.L. et al. Nat Commun (2023) 14:6992-6992. DOI 10.1038/s41467-023-42395-z · PubMed

Other PDB entries of the same protein (UniProt Q93034 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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