1HV2: Yeast elongin C

Solution structure of yeast elongin C in complex with a von hippel-lindau peptide. Determined by solution NMR. Released 6 Sept 2001.

Method
Solution NMR
Organism
Saccharomyces cerevisiae
Chains
2
Atoms
918
Mol. weight
13.11 kDa
Released
6 Sept 2001

Explore 1HV2 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1HV2 contains 6 α-helices and 5 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: 5 helices, 5 β-strands

ElementResiduesLengthSheet
β-strand5-1061
β-strand14-1961
α-helix20-234
α-helix27-348
β-strand43-4641
β-strand4712
β-strand4912
α-helix51-7020
α-helix77-793
α-helix84-9714
Chain B: 1 helix, 0 β-strands
ElementResiduesLengthSheet
α-helix158-17013

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Elongin CAprotein99Saccharomyces cerevisiaeQ03071 (AlphaFold model)
Von hippel-lindau disease tumor suppressorBprotein15P40338 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>1HV2_1 ELONGIN C (chains A)
MSQDFVTLVSKDDKEYEISRSAAMISPTLKAMIEGPFRESKGRIELKQFDSHILEKAVEY
LNYNLKYSGVSEDDDEIPEFEIPTEMSLELLLAADYLSI
Sequence of entity 2 (B), FASTA
>1HV2_2 VON HIPPEL-LINDAU DISEASE TUMOR SUPPRESSOR (chains B)
TLKERCLQVVRSLVK

Primary citation

Solution structure and dynamics of yeast elongin C in complex with a von Hippel-Lindau peptide. Botuyan, M.V., Mer, G., Yi, G.S. et al. J Mol Biol (2001) 312:177-186. DOI 10.1006/jmbi.2001.4938 · PubMed

Other PDB entries of the same protein (UniProt Q03071 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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