5LAS: Egl nine homolog 1

HIF prolyl hydroxylase 2 (PHD2-R281C/P317C/R396T) cross-linked to HIF-1alpha NODD-L397C/D412C and N-oxalylglycine (NOG) (complex-3). Determined by X-ray diffraction at 2.1 Å resolution. Released 31 Aug 2016.

Method
X-ray diffraction
Resolution
2.1 Å
Organism
Homo sapiens
Chains
4
Atoms
3,751
Mol. weight
59.94 kDa
Ligands
MN, OGA
Released
31 Aug 2016

Explore 5LAS in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5LAS contains 20 α-helices and 39 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.

Chain A: 8 helices, 17 β-strands

ElementResiduesLengthSheet
α-helix190-1934
α-helix194-1985
α-helix199-2057
β-strand207-21041
α-helix216-23116
β-strand236-23721
β-strand24012
β-strand25213
β-strand255-25951
α-helix267-28115
β-strand292-29541
α-helix296-2972
β-strand298-30471
β-strand308-31363
β-strand322-32981
β-strand33114
α-helix336-3394
β-strand34013
β-strand343-34533
β-strand354-35633
β-strand35914
β-strand362-36761
β-strand374-37963
β-strand382-392111
α-helix393-40210
Chain B: 8 helices, 18 β-strands
ElementResiduesLengthSheet
α-helix191-1933
α-helix194-1985
α-helix199-2057
β-strand207-21045
α-helix216-23116
β-strand236-23725
β-strand24016
β-strand25217
β-strand255-25955
α-helix267-28115
β-strand292-29545
α-helix296-2972
β-strand298-30475
β-strand310-31347
β-strand322-32985
β-strand33118
α-helix336-3394
β-strand34019
β-strand343-34537
β-strand354-35637
β-strand35918
β-strand362-36765
β-strand374-37637
β-strand37919
β-strand382-392115
α-helix393-3997
Chains C and D: 2 helices, 2 β-strands
ElementResiduesLengthSheet
α-helix397-3993
β-strand40212
α-helix4031
β-strand409-41021

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Egl nine homolog 1A, Bprotein252Homo sapiensQ9GZT9 (AlphaFold model)
Hypoxia-inducible factor 1-alphaC, Dprotein19Homo sapiensQ16665 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>5LAS_1 Egl nine homolog 1 (chains A, B)
GSHMASPNGQTKPLPALKLALEYIVPAMNKHGICVVDDFLGKETGQQIGDEVRALHDTGK
FTDGQLVSQKSDSSKDIRGDKITWIEGKEPGCETIGLLMSSMDDLICHCNGKLGSYKING
RTKAMVACYPGNGTGYVRHVDNCNGDGRCVTCIYYLNKDWDAKVSGGILRIFPEGKAQFA
DIEPKFDRLLFFWSDRRNPHEVQPAYATRYAITVWYFDADETAAAKVKYLTGEKGVRVEL
NKPSDSVGKDVF
Sequence of entity 2 (C, D), FASTA
>5LAS_2 Hypoxia-inducible factor 1-alpha (chains C, D)
DACTLLAPAAGDTIISLCF

Ligands and cofactors

IDNameFormulaCopies
MNManganese (II) ionMn2
OGAN-oxalylglycineC4 H5 N O52

Primary citation

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:

Browse structure collections

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