Structure of PDB 5lbe Chain A Binding Site BS03

Receptor Information
>5lbe Chain A (length=220) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
LPALKLALEYIVPCMNKHGICVVDDFLGKETGQQIGDEVRALHDTGKFTD
GQLVSQDSSKDIRGDKITWIEGKEPGCETIGLLMSSMDDLIRHCNGKLGS
YKINERTKAMVACYPGNGTGYVRHVDNPNGDGRCVTCIYYLNKDWDAKVS
GGILRIFPEGKAQFADIEPKFDRLLFFWSDRRNPHEVQPAYATRYAITVW
YFDADERARAKVKYLGVRVE
Ligand information
Ligand IDBCT
InChIInChI=1S/CH2O3/c2-1(3)4/h(H2,2,3,4)/p-1
InChIKeyBVKZGUZCCUSVTD-UHFFFAOYSA-M
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0C(=O)(O)[O-]
CACTVS 3.341OC([O-])=O
ACDLabs 10.04[O-]C(=O)O
FormulaC H O3
NameBICARBONATE ION
ChEMBL
DrugBank
ZINC
PDB chain5lbe Chain A Residue 503 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB5lbe Structural basis for oxygen degradation domain selectivity of the HIF prolyl hydroxylases.
Resolution1.749 Å
Binding residue
(original residue number in PDB)
R312 P373
Binding residue
(residue number reindexed from 1)
R123 P184
Annotation score2
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
PDBsum5lbe
PubMed27561929
UniProtQ9GZT9|EGLN1_HUMAN Egl nine homolog 1 (Gene Name=EGLN1)

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