Crystal structure of a hydroxylated HIF-1 alpha peptide bound to the pVHL/elongin-C/elongin-B complex. Determined by X-ray diffraction at 2.0 Å resolution. Released 3 Jul 2002.
Explore 1LQB in 3D Show helices and sheets RCSB PDB PDBe
1LQB contains 17 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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 2-9 | 8 | 1 |
| β-strand | 10 | 1 | 2 |
| β-strand | 12-19 | 8 | 1 |
| β-strand | 23 | 1 | 3 |
| α-helix | 24-35 | 12 | |
| α-helix | 39-41 | 3 | |
| β-strand | 42-46 | 5 | 1 |
| β-strand | 49-50 | 2 | 1 |
| α-helix | 51-52 | 2 | |
| β-strand | 56 | 1 | 3 |
| β-strand | 68 | 1 | 4 |
| β-strand | 71 | 1 | 4 |
| α-helix | 72 | 1 | |
| β-strand | 73-79 | 7 | 1 |
| β-strand | 90 | 1 | 2 |
| α-helix | 98-100 | 3 | |
| α-helix | 101-103 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 18-22 | 5 | 1 |
| β-strand | 28-32 | 5 | 1 |
| α-helix | 33-36 | 4 | |
| α-helix | 40-45 | 6 | |
| β-strand | 59-61 | 3 | 1 |
| α-helix | 67-83 | 17 | |
| α-helix | 89-92 | 4 | |
| α-helix | 97-99 | 3 | |
| α-helix | 100-110 | 11 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 71-78 | 8 | 5 |
| β-strand | 84-89 | 6 | 6 |
| β-strand | 95-97 | 3 | 6 |
| β-strand | 101 | 1 | 6 |
| β-strand | 105-112 | 8 | 5 |
| β-strand | 116-121 | 6 | 6 |
| β-strand | 127 | 1 | 6 |
| β-strand | 129-130 | 2 | 5 |
| β-strand | 133 | 1 | 5 |
| β-strand | 136 | 1 | 6 |
| α-helix | 146 | 1 | |
| β-strand | 147-152 | 6 | 5 |
| α-helix | 158-169 | 12 | |
| α-helix | 172-177 | 6 | |
| α-helix | 183-189 | 7 | |
| α-helix | 194-207 | 14 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 565 | 1 | 5 |
| β-strand | 572-573 | 2 | 5 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Elongin B | A | protein | 118 | Homo sapiens | Q15370 (AlphaFold model) |
| Elongin C | B | protein | 96 | Homo sapiens | Q15369 (AlphaFold model) |
| von hippel-lindau disease tumor supressor | C | protein | 162 | Homo sapiens | P40337 (AlphaFold model) |
| Hypoxia-inducible factor 1 ALPHA | D | protein | 34 | Q16665 (AlphaFold model) |
>1LQB_1 Elongin B (chains A) MDVFLMIRRHKTTIFTDAKESSTVFELKRIVEGILKRPPDEQRLYKDDQLLDDGKTLGEC GFTSQTARPQAPATVGLAFRADDTFEALCIEPFSSPPELPDVMKPQDSGSSANEQAVQ
>1LQB_2 Elongin C (chains B) MYVKLISSDGHEFIVKREHALTSGTIKAMLSGPGQFAENETNEVNFREIPSHVLSKVCMY FTYKVRYTNSSTEIPEFPIAPEIALELLMAANFLDC
>1LQB_3 von hippel-lindau disease tumor supressor (chains C) GSMEAGRPRPVLRSVNSREPSQVIFCNRSPRVVLPVWLNFDGEPQPYPTLPPGTGRRIHS YRGHLWLFRDAGTHDGLLVNQTELFVPSLNVDGQPIFANITLPVYTLKERCLQVVRSLVK PENYRRLDIVRSLYEDLEDHPNVQKDLERLTQERIAHQRMGD
>1LQB_4 Hypoxia-inducible factor 1 ALPHA (chains D) PFSTQDTDLDLEMLAPYIPMDDDFQLRSFDQLSP
Structural basis for the recognition of hydroxyproline in HIF-1 alpha by pVHL. Hon, W.C., Wilson, M.I., Harlos, K. et al. Nature (2002) 417:975-978. DOI 10.1038/nature00767 · PubMed
Other PDB entries of the same protein (UniProt Q15370 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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