Structure of PDB 5las Chain A

Receptor sequence

>5lasA (length=215) Species: 9606 (Homo sapiens)

PALKLALEYIVPAMNKHGICVVDDFLGKETGQQIGDEVRALHDTGKFTDG
QLVSQKSDSSKDIRGDKITWIEGKEPGCETIGLLMSSMDDLICHCNGKLG
SYKINGRTKAMVACYPGNGTGYVRHVDNCNGDGRCVTCIYYLNKDWDAKV
SGGILRIFPEGKAQFADIEPKFDRLLFFWSDRRNPHEVQPAYATRYAITV
WYFDADETAAAKVKY

3D structure

• PDB: 5las Structural basis for oxygen degradation domain selectivity of the HIF prolyl hydroxylases.
• Chain: A
• Resolution: 2.1 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	A	Q239 L240 V241 S242 K244 R252 W258 D277 C281 N284 I292 N293 G294 R295 Y310 H313 D315 C317 R322 R370 W389 Y390 F391	Q51 L52 V53 S54 K56 R64 W70 D89 C93 N96 I104 N105 G106 R107 Y122 H125 D127 C129 R134 R182 W201 Y202 F203
BS02	peptide	A	S245 S247 D250	S57 S59 D62
BS03	MN	A	H313 D315 H374	H125 D127 H186

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