Structure of PDB 5lbb Chain A

Receptor sequence
>5lbbA (length=229) Species: 9606 (Homo sapiens) [Search protein sequence]
NGQTLPALKLALEYIVPCMNKHGICVVDDFLGKETGQQIGDEVRALHDTG
KFTDGQLVSQKSDSSKDIRGDKITWIEGKEPGCETIGLLMSSMDDLIRHC
NGKLGSYKINGRTKAMVACYPGNGTGYVRHVDNPNGDGRCVTCIYYLNKD
WDAKVSGGILRIFPEGKAQFADIEPKFDRLLFFWSDRRNPHEVQPAYATR
YAITVWYFDADETARAKVKYLTGGVRVEL
3D structure
PDB5lbb Structural basis for oxygen degradation domain selectivity of the HIF prolyl hydroxylases.
ChainA
Resolution1.7 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 H130 D132 H191
BS02 UN9 A D254 M299 Y303 Y310 H313 Y329 H374 V376 R383 D71 M116 Y120 Y127 H130 Y146 H191 V193 R200 BindingDB: IC50=300nM,EC50=79000nM,Kd=80nM
BS03 BCT A R312 P373 R129 P190
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:5lbb, PDBe:5lbb, PDBj:5lbb
PDBsum5lbb
PubMed27561929
UniProtQ9GZT9|EGLN1_HUMAN Egl nine homolog 1 (Gene Name=EGLN1)

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