HIF prolyl hydroxylase 2 (PHD2/EGLN1) R371H variant in complex with Mn(II) and N-[(1-chloro-4-hydroxyisoquinolin-3-yl)carbonyl]glycine (IOX3/UN9). Determined by X-ray diffraction at 1.7 Å resolution. Released 31 Aug 2016.
Explore 5LB6 in 3D Show helices and sheets RCSB PDB PDBe
5LB6 contains 9 α-helices and 17 β-strands across 1 chain. 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 |
|---|---|---|---|
| α-helix | 190-193 | 4 | |
| α-helix | 194-198 | 5 | |
| α-helix | 199-205 | 7 | |
| β-strand | 207-210 | 4 | 1 |
| α-helix | 216-231 | 16 | |
| β-strand | 240-242 | 3 | 2 |
| α-helix | 247-249 | 3 | |
| β-strand | 251-252 | 2 | 2 |
| β-strand | 255-259 | 5 | 1 |
| α-helix | 267-282 | 16 | |
| β-strand | 292-295 | 4 | 1 |
| α-helix | 296-297 | 2 | |
| β-strand | 298-303 | 6 | 1 |
| β-strand | 310-313 | 4 | 3 |
| β-strand | 322-329 | 8 | 1 |
| β-strand | 331 | 1 | 4 |
| α-helix | 336-339 | 4 | |
| β-strand | 340 | 1 | 5 |
| β-strand | 343-345 | 3 | 3 |
| β-strand | 354-356 | 3 | 3 |
| β-strand | 359 | 1 | 4 |
| β-strand | 362-367 | 6 | 1 |
| β-strand | 374-376 | 3 | 3 |
| β-strand | 379 | 1 | 5 |
| β-strand | 383-392 | 10 | 1 |
| α-helix | 393-402 | 10 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Egl nine homolog 1 | A | protein | 252 | Homo sapiens | Q9GZT9 (AlphaFold model) |
>5LB6_1 Egl nine homolog 1 (chains A) GSHMASPNGQTKPLPALKLALEYIVPCMNKHGICVVDDFLGKETGQQIGDEVRALHDTGK FTDGQLVSQKSDSSKDIRGDKITWIEGKEPGCETIGLLMSSMDDLIRHCNGKLGSYKING RTKAMVACYPGNGTGYVRHVDNPNGDGRCVTCIYYLNKDWDAKVSGGILRIFPEGKAQFA DIEPKFDRLLFFWSDRHNPHEVQPAYATRYAITVWYFDADERARAKVKYLTGEKGVRVEL NKPSDSVGKDVF
| ID | Name | Formula | Copies |
|---|---|---|---|
| UN9 | N-[(1-chloro-4-hydroxyisoquinolin-3-yl)carbonyl]glycine | C12 H9 Cl N2 O4 | 1 |
| MN | Manganese (II) ion | Mn | 1 |
Water and common crystallization additives (GOL, SO4) are not listed.
Structural basis for oxygen degradation domain selectivity of the HIF prolyl hydroxylases. Chowdhury, R., Leung, I.K., Tian, Y.M. et al. Nat Commun (2016) 7:12673-12673. DOI 10.1038/ncomms12673 · PubMed
Other PDB entries of the same protein (UniProt Q9GZT9 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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