Structure of PDB 5l9b Chain A Binding Site BS04
Receptor Information
>5l9b Chain A (length=222) Species:
9606
(Homo sapiens) [
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LPALKLALEYIVPAMNKHGICVVDDFLGKETGQQIGDEVRALHDTGKFTD
GQLVSQKSDSSKDIRGDKITWIEGKEPGCETIGLLMSSMDDLIRHCNGKL
GSYKINGRTKAMVACYPGNGTGYVRHVDNPNGDGRCVTCIYYLNKDWDAK
VSGGILRIFPEGKAQFADIEPKFDRLLFFWSDRRNPHEVQPAYATRYAIT
VWYFDADERAAAKVKYLTGEKG
Ligand information
Ligand ID
AKG
InChI
InChI=1S/C5H6O5/c6-3(5(9)10)1-2-4(7)8/h1-2H2,(H,7,8)(H,9,10)
InChIKey
KPGXRSRHYNQIFN-UHFFFAOYSA-N
SMILES
Software
SMILES
ACDLabs 10.04
O=C(O)C(=O)CCC(=O)O
OpenEye OEToolkits 1.7.6
C(CC(=O)O)C(=O)C(=O)O
CACTVS 3.385
OC(=O)CCC(=O)C(O)=O
Formula
C5 H6 O5
Name
2-OXOGLUTARIC ACID
ChEMBL
CHEMBL1686
DrugBank
DB08845
ZINC
ZINC000001532519
PDB chain
5l9b Chain A Residue 502 [
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Receptor-Ligand Complex Structure
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PDB
5l9b
Structural basis for oxygen degradation domain selectivity of the HIF prolyl hydroxylases.
Resolution
1.95 Å
Binding residue
(original residue number in PDB)
Y310 H313 Y329 L343 H374 V376 R383
Binding residue
(residue number reindexed from 1)
Y123 H126 Y142 L156 H187 V189 R196
Annotation score
5
Enzymatic activity
Enzyme Commision number
1.14.11.29
: hypoxia-inducible factor-proline dioxygenase.
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:5l9b
,
PDBe:5l9b
,
PDBj:5l9b
PDBsum
5l9b
PubMed
27561929
UniProt
Q9GZT9
|EGLN1_HUMAN Egl nine homolog 1 (Gene Name=EGLN1)
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