Structure of PDB 5am2 Chain A Binding Site BS02

Receptor Information
>5am2 Chain A (length=537) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
TLRAAVFDLDGVLALPAVFGVLGRTEEALALPRGLLNDAFQKGGPEGATT
RLMKGEITLSQWIPLMEENCRKCSETAKVFSIKEIFDKAISARKINRPML
QAALMLRKKGFTTAILTNTWLDDRAERDGLAQLMCELKMHFDFLIESCQV
GMVKPEPQIYKFLLDTLKASPSEVVFLDDIGANLKPARDLGMVTILVQDT
DTALKELEKVTGIQLLNTPAPLPTSCNPSDMSHGYVTVKPRVRLHFVELG
SGPAVCLCHGFPESWYSWRYQIPALAQAGYRVLAMDMKGYGESSAPPEIE
EYCMEVLCKEMVTFLDKLGLSQAVFIGHDWGGMLVWYMALFYPERVRAVA
SLNTPFIPANPNMSPLESIKANPVFDYQLYFQEPGVAEAELEQNLSRTFK
SLFRASDESVLVCEAGGLFVNSPEEPSLSRMVTEEEIQFYVQQFKKSGFR
GPLNWYRNMERNWKWACKSLGRKILIPALMVTAEKDFVLVPQMSQHMEDW
IPHLKRGHIEDCGHWTQMDKPTEVNQILIKWLDSDAR
Ligand information
Ligand IDKUF
InChIInChI=1S/C10H9NO/c1-7-2-3-8-4-5-11-10(12)9(8)6-7/h2-6H,1H3,(H,11,12)
InChIKeyZLTCEYHTNOZGIS-UHFFFAOYSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.7.6Cc1ccc2c(c1)C(=O)NC=C2
CACTVS 3.385Cc1ccc2C=CNC(=O)c2c1
FormulaC10 H9 N O
Name7-METHYL-2H-ISOQUINOLIN-1-ONE
ChEMBL
DrugBank
ZINCZINC000034628558
PDB chain5am2 Chain A Residue 1553 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB5am2 Successful Generation of Structural Information for Fragment-Based Drug Discovery.
Resolution1.7 Å
Binding residue
(original residue number in PDB)		D496 F497 V498 H524 W525
Binding residue
(residue number reindexed from 1)		D486 F487 V488 H514 W515
Annotation score1
Binding affinityMOAD: ic50=9.685uM
PDBbind-CN: -logKd/Ki=5.01,IC50=9.685uM
Enzymatic activity
Catalytic site (original residue number in PDB) F267 H334 D335 W336 N359 N378 Y383 Y466 D496 H524
Catalytic site (residue number reindexed from 1) F261 H328 D329 W330 N353 N372 Y377 Y456 D486 H514
Enzyme Commision number 3.1.3.76: lipid-phosphate phosphatase.
3.3.2.10: soluble epoxide hydrolase.
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0003824 catalytic activity
GO:0004301 epoxide hydrolase activity
GO:0015643 toxic substance binding
GO:0016787 hydrolase activity
GO:0016791 phosphatase activity
GO:0033885 10-hydroxy-9-(phosphonooxy)octadecanoate phosphatase activity
GO:0042577 lipid phosphatase activity
GO:0042803 protein homodimerization activity
GO:0046872 metal ion binding
GO:0052642 lysophosphatidic acid phosphatase activity
Biological Process
GO:0006629 lipid metabolic process
GO:0009056 catabolic process
GO:0009636 response to toxic substance
GO:0010628 positive regulation of gene expression
GO:0016311 dephosphorylation
GO:0042632 cholesterol homeostasis
GO:0046272 stilbene catabolic process
GO:0046839 phospholipid dephosphorylation
GO:0090181 regulation of cholesterol metabolic process
GO:0097176 epoxide metabolic process
Cellular Component
GO:0005737 cytoplasm
GO:0005777 peroxisome
GO:0005782 peroxisomal matrix
GO:0005829 cytosol
GO:0070062 extracellular exosome

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:5am2, PDBe:5am2, PDBj:5am2
PDBsum5am2
PubMed25931264
UniProtP34913|HYES_HUMAN Bifunctional epoxide hydrolase 2 (Gene Name=EPHX2)

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