Crystal structure of a hydroxylated hif-1 alpha peptide bound to the PVHL/ELONGIN-C/ELONGIN-B complex

Structure

x-ray diffraction · 4 distinct chains · 27% helix, 26% strand (DSSP).

Ligands and binding sites

• SO4 · Sulfate ion · ion · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Interfaces

5 interfaces between chains.

• A–B · 1193 Ų buried · 13 hydrogen bonds · protein-protein
• B–C · 1070 Ų buried · 11 hydrogen bonds · protein-protein
• C–D · 975 Ų buried · 17 hydrogen bonds · protein-protein
• A–C · 189 Ų buried · 1 hydrogen bond · protein-protein
• B–D · 59 Ų buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 modified (hydroxylation).

Compared structures

• 1LQB · Crystal structure of a hydroxylated HIF-1 alpha peptide bound to the… · the same entry in another collection · chain D against D, TM-score 1.00
• P40337 · AlphaFold monomer V2.0 prediction for von hippel-lindau disease tumor suppressor (P40337) · a predicted model of the same protein · chain C against A, TM-score 0.99
• Q15370 · AlphaFold monomer V2.0 prediction for elongin-B (Q15370) · a predicted model of the same protein · chain A against A, TM-score 0.97
• Q15369 · AlphaFold monomer V2.0 prediction for elongin-C (Q15369) · a predicted model of the same protein · chain B against A, TM-score 0.96
• Q16665 · AlphaFold monomer V2.0 prediction for hypoxia-inducible factor 1-alpha (Q16665) · a predicted model of the same protein · chain D against A, TM-score 0.23

Analyse

• Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
• Every structure of UniProt Q15370
• Every structure of UniProt Q15369
• Every structure of UniProt P40337
• Every structure of UniProt Q16665
• Elsewhere: RCSB PDB 1LQB · PDBe 1LQB · UniProt Q15370 · UniProt Q15369 · UniProt P40337 · UniProt Q16665