Structure of PDB 5la9 Chain B

Receptor sequence

>5la9B (length=212) Species: 9606 (Homo sapiens)

LPALKLALEYIVPAMNKHGICVVDDFLGKETGQQIGDEVRALHDTGKFTD
GQLVKDIRGDKITWIEGKEPGCETIGLLMSSMDDLICHCNGKLGSYKING
RTKAMVACYPGNGTGYVRHCDNPNGDGRCVTCIYYLNKDWDAKVSGGILR
IFPEGKAQFADIEPKFDRLLFFWSDRRNPHEVQPAYATRYAITVWYFDAD
ERAAAKVKYLTG

3D structure

• PDB: 5la9 Structural basis for oxygen degradation domain selectivity of the HIF prolyl hydroxylases.
• Chain: B
• Resolution: 2.813 Å

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	peptide	B	N306 G307 P378	N112 G113 P184
BS02	peptide	B	Q239 L240 V241 W258 D277 C281 N284 I292 N293 G294 R295 T296 Y310 R312 H313 C314 D315 P317 R322 R370 W389 F391	Q52 L53 V54 W64 D83 C87 N90 I98 N99 G100 R101 T102 Y116 R118 H119 C120 D121 P123 R128 R176 W195 F197
BS03	MN	B	H313 D315 H374	H119 D121 H180

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

External links

• PDB: RCSB:5la9, PDBe:5la9, PDBj:5la9
• PDBsum: 5la9
• PubMed: 27561929
• UniProt: Q9GZT9|EGLN1_HUMAN Egl nine homolog 1 (Gene Name=EGLN1)