Solution structure of yeast elongin C in complex with a von hippel-lindau peptide. Determined by solution NMR. Released 6 Sept 2001.
Explore 1HV2 in 3D Show helices and sheets RCSB PDB PDBe
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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 5-10 | 6 | 1 |
| β-strand | 14-19 | 6 | 1 |
| α-helix | 20-23 | 4 | |
| α-helix | 27-34 | 8 | |
| β-strand | 43-46 | 4 | 1 |
| β-strand | 47 | 1 | 2 |
| β-strand | 49 | 1 | 2 |
| α-helix | 51-70 | 20 | |
| α-helix | 77-79 | 3 | |
| α-helix | 84-97 | 14 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 158-170 | 13 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Elongin C | A | protein | 99 | Saccharomyces cerevisiae | Q03071 (AlphaFold model) |
| Von hippel-lindau disease tumor suppressor | B | protein | 15 | P40338 (AlphaFold model) |
>1HV2_1 ELONGIN C (chains A) MSQDFVTLVSKDDKEYEISRSAAMISPTLKAMIEGPFRESKGRIELKQFDSHILEKAVEY LNYNLKYSGVSEDDDEIPEFEIPTEMSLELLLAADYLSI
>1HV2_2 VON HIPPEL-LINDAU DISEASE TUMOR SUPPRESSOR (chains B) TLKERCLQVVRSLVK
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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