Structure of PDB 5lbc Chain A

Receptor sequence
>5lbcA (length=222) Species: 9606 (Homo sapiens) [Search protein sequence]
LPALKLALEYIVPCMNKHGICVVDDFLGKETGQQIGDEVRALHDTGKFTD
GQLVSQKSDSSKDIRGDKITWIEGKEPGCETIGLLMSSMDDLVLHCNGKL
GSYKVNGRTKAMVACYPGNGTGYVRHVDNPNGDGRCVTCIYYLNKDWDAK
VSGGILRIFPEGKAQFADIEPKFDRLLFFWSDRRNPHEVQPAYATRYAIT
VWYFDADERARAKVKYLVRVEL
3D structure
PDB5lbc Structural basis for oxygen degradation domain selectivity of the HIF prolyl hydroxylases.
ChainA
Resolution1.816 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 1.14.11.29: hypoxia-inducible factor-proline dioxygenase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 MN A H313 D315 H374 H126 D128 H187
BS02 UN9 A D254 M299 Y303 Y310 H313 Y329 L343 H374 V376 R383 D67 M112 Y116 Y123 H126 Y142 L156 H187 V189 R196 BindingDB: IC50=300nM,EC50=79000nM,Kd=80nM
BS03 BCT A R312 P373 R125 P186
Gene Ontology
Molecular Function
GO:0005506 iron ion binding
GO:0016705 oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
GO:0031418 L-ascorbic acid binding

View graph for
Molecular Function
External links
PDB RCSB:5lbc, PDBe:5lbc, PDBj:5lbc
PDBsum5lbc
PubMed27561929
UniProtQ9GZT9|EGLN1_HUMAN Egl nine homolog 1 (Gene Name=EGLN1)

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