Structure of PDB 5lbe Chain A Binding Site BS03
Receptor Information
>5lbe Chain A (length=220) Species:
9606
(Homo sapiens) [
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LPALKLALEYIVPCMNKHGICVVDDFLGKETGQQIGDEVRALHDTGKFTD
GQLVSQDSSKDIRGDKITWIEGKEPGCETIGLLMSSMDDLIRHCNGKLGS
YKINERTKAMVACYPGNGTGYVRHVDNPNGDGRCVTCIYYLNKDWDAKVS
GGILRIFPEGKAQFADIEPKFDRLLFFWSDRRNPHEVQPAYATRYAITVW
YFDADERARAKVKYLGVRVE
Ligand information
Ligand ID
BCT
InChI
InChI=1S/CH2O3/c2-1(3)4/h(H2,2,3,4)/p-1
InChIKey
BVKZGUZCCUSVTD-UHFFFAOYSA-M
SMILES
Software
SMILES
OpenEye OEToolkits 1.5.0
C(=O)(O)[O-]
CACTVS 3.341
OC([O-])=O
ACDLabs 10.04
[O-]C(=O)O
Formula
C H O3
Name
BICARBONATE ION
ChEMBL
DrugBank
ZINC
PDB chain
5lbe Chain A Residue 503 [
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Receptor-Ligand Complex Structure
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PDB
5lbe
Structural basis for oxygen degradation domain selectivity of the HIF prolyl hydroxylases.
Resolution
1.749 Å
Binding residue
(original residue number in PDB)
R312 P373
Binding residue
(residue number reindexed from 1)
R123 P184
Annotation score
2
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:5lbe
,
PDBe:5lbe
,
PDBj:5lbe
PDBsum
5lbe
PubMed
27561929
UniProt
Q9GZT9
|EGLN1_HUMAN Egl nine homolog 1 (Gene Name=EGLN1)
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