Structure of PDB 6yw1 Chain A Binding Site BS03
Receptor Information
>6yw1 Chain A (length=209) Species:
9606
(Homo sapiens) [
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KPLPALKLALEYIVPCMNKHGICVVDDFLGKETGQQIGDEVRALHDTGKF
TDGQDIRGDKITWIEGKEPGCETIGLLMSSMDDLIRHCNGKLGSYKINGR
TKAMVACYPGNGTGYVRHVDNPNGDGRCVTCIYYLNKDWDAKVSGGILRI
FPEGKAQFADIEPKFDRLLFFWSDRRNPHEVQPAYATRYAITVWYFDADE
RARAKVKYL
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
6yw1 Chain A Residue 502 [
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Receptor-Ligand Complex Structure
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PDB
6yw1
Use of cyclic peptides to induce crystallization: case study with prolyl hydroxylase domain 2.
Resolution
1.46 Å
Binding residue
(original residue number in PDB)
Y310 H313 Y329 H374 V376 R383
Binding residue
(residue number reindexed from 1)
Y115 H118 Y134 H179 V181 R188
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:6yw1
,
PDBe:6yw1
,
PDBj:6yw1
PDBsum
6yw1
PubMed
33319810
UniProt
Q9GZT9
|EGLN1_HUMAN Egl nine homolog 1 (Gene Name=EGLN1)
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