6GFX: PVHL:EloB:EloC

pVHL:EloB:EloC in complex with modified HIF-1a CODD peptide containing (3R,4S)-3-fluoro-4-hydroxyproline (ligand 13a). Determined by X-ray diffraction at 1.83 Å resolution. Released 11 Jul 2018.

Method
X-ray diffraction
Resolution
1.83 Å
Organism
Homo sapiens
Chains
4
Atoms
3,138
Mol. weight
43.56 kDa
Released
11 Jul 2018

Explore 6GFX in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6GFX contains 22 α-helices and 27 β-strands across 4 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: 8 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-helix64-663
β-strand6814
β-strand7114
α-helix721
β-strand73-7971
α-helix86-883
β-strand9012
α-helix96-1005
α-helix101-1033
Chain B: 6 helices, 3 β-strands
ElementResiduesLengthSheet
β-strand18-2251
β-strand28-3251
α-helix33-364
α-helix40-467
β-strand59-6131
α-helix67-8317
α-helix89-924
α-helix97-993
α-helix100-11011
Chain C: 8 helices, 11 β-strands
ElementResiduesLengthSheet
β-strand71-7885
α-helix831
β-strand84-8966
β-strand95-9736
β-strand10116
β-strand105-11285
β-strand116-12166
β-strand12716
β-strand129-13025
β-strand13315
β-strand13616
α-helix140-1412
α-helix142-1443
α-helix145-1462
β-strand147-15265
α-helix158-16912
α-helix172-1776
α-helix183-1897
α-helix194-20613
Chain D: 0 helices, 2 β-strands
ElementResiduesLengthSheet
β-strand56515
β-strand572-57325

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Elongin-BAprotein104Homo sapiensQ15370 (AlphaFold model)
Elongin-CBprotein97Homo sapiensQ15369 (AlphaFold model)
von Hippel-Lindau disease tumor suppressorCprotein160Homo sapiensP40337 (AlphaFold model)
Fluorinated hypoxia-inducible factor 1 alpha peptideDprotein19Homo sapiensQ16665 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>6GFX_1 Elongin-B (chains A)
MDVFLMIRRHKTTIFTDAKESSTVFELKRIVEGILKRPPDEQRLYKDDQLLDDGKTLGEC
GFTSQTARPQAPATVGLAFRADDTFEALCIEPFSSPPELPDVMK
Sequence of entity 2 (B), FASTA
>6GFX_2 Elongin-C (chains B)
MMYVKLISSDGHEFIVKREHALTSGTIKAMLSGPGQFAENETNEVNFREIPSHVLSKVCM
YFTYKVRYTNSSTEIPEFPIAPEIALELLMAANFLDC
Sequence of entity 3 (C), FASTA
>6GFX_3 von Hippel-Lindau disease tumor suppressor (chains C)
MEAGRPRPVLRSVNSREPSQVIFCNRSPRVVLPVWLNFDGEPQPYPTLPPGTGRRIHSYR
GHLWLFRDAGTHDGLLVNQTELFVPSLNVDGQPIFANITLPVYTLKERCLQVVRSLVKPE
NYRRLDIVRSLYEDLEDHPNVQKDLERLTQERIAHQRMGD
Sequence of entity 4 (D), FASTA
>6GFX_4 FLUORINATED HYPOXIA-INDUCIBLE FACTOR 1 ALPHA PEPTIDE (chains D)
DEALAXYIPMDDDFQLRSF

Primary citation

3-Fluoro-4-hydroxyprolines: Synthesis, Conformational Analysis, and Stereoselective Recognition by the VHL E3 Ubiquitin Ligase for Targeted Protein Degradation. Testa, A., Lucas, X., Castro, G.V. et al. J Am Chem Soc (2018) 140:9299-9313. DOI 10.1021/jacs.8b05807 · PubMed

Other PDB entries of the same protein (UniProt Q15370 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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