Structure of PDB 2y34 Chain A

Receptor sequence
>2y34A (length=216) Species: 9606 (Homo sapiens) [Search protein sequence]
PLPALKLALEYIVPCMNKHGICVVDDFLGKETGQQIGDEVRALHDTGKFT
DGQLVSQKSDSSKDIRGDKITWIEGKEPGCETIGLLMSSMDDLIRHCNGK
LGSYKINGRTKAMVACYPGNGTGYVRHVDNPNGDGRCVTCIYYLNKDWDA
KVSGGILRIFPEGKAQFADIEPKFDRLLFFWSDRRNPHEVQPAYATRYAI
TVWYFDADERARAKVK
3D structure
PDB2y34 Studies on the reaction of nitric oxide with the hypoxia-inducible factor prolyl hydroxylase domain 2 (EGLN1).
ChainA
Resolution2.01 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 FE2 A H313 D315 H374 H127 D129 H188
BS02 UN9 A D254 M299 Y303 Y310 H313 Y329 L343 H374 V376 R383 D68 M113 Y117 Y124 H127 Y143 L157 H188 V190 R197 PDBbind-CN: -logKd/Ki=7.10,Kd=80nM
BindingDB: IC50=300nM,EC50=79000nM,Kd=80nM
BS03 UN9 A W258 T296 D320 F391 W72 T110 D134 F205 PDBbind-CN: -logKd/Ki=7.10,Kd=80nM
BindingDB: IC50=300nM,EC50=79000nM,Kd=80nM
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:2y34, PDBe:2y34, PDBj:2y34
PDBsum2y34
PubMed21601578
UniProtQ9GZT9|EGLN1_HUMAN Egl nine homolog 1 (Gene Name=EGLN1)

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