Structure of PDB 5am2 Chain A

Receptor sequence
>5am2A (length=537) Species: 9606 (Homo sapiens) [Search protein sequence]
TLRAAVFDLDGVLALPAVFGVLGRTEEALALPRGLLNDAFQKGGPEGATT
RLMKGEITLSQWIPLMEENCRKCSETAKVFSIKEIFDKAISARKINRPML
QAALMLRKKGFTTAILTNTWLDDRAERDGLAQLMCELKMHFDFLIESCQV
GMVKPEPQIYKFLLDTLKASPSEVVFLDDIGANLKPARDLGMVTILVQDT
DTALKELEKVTGIQLLNTPAPLPTSCNPSDMSHGYVTVKPRVRLHFVELG
SGPAVCLCHGFPESWYSWRYQIPALAQAGYRVLAMDMKGYGESSAPPEIE
EYCMEVLCKEMVTFLDKLGLSQAVFIGHDWGGMLVWYMALFYPERVRAVA
SLNTPFIPANPNMSPLESIKANPVFDYQLYFQEPGVAEAELEQNLSRTFK
SLFRASDESVLVCEAGGLFVNSPEEPSLSRMVTEEEIQFYVQQFKKSGFR
GPLNWYRNMERNWKWACKSLGRKILIPALMVTAEKDFVLVPQMSQHMEDW
IPHLKRGHIEDCGHWTQMDKPTEVNQILIKWLDSDAR
3D structure
PDB5am2 Successful Generation of Structural Information for Fragment-Based Drug Discovery.
ChainA
Resolution1.7 Å
3D
structure
Catalytic site residues are labeled in the structure
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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.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 KUF A F267 Y383 F387 L408 L428 F261 Y377 F381 L402 L418 MOAD: ic50=9.685uM
PDBbind-CN: -logKd/Ki=5.01,IC50=9.685uM
BS02 KUF A D496 F497 V498 H524 W525 D486 F487 V488 H514 W515 MOAD: ic50=9.685uM
PDBbind-CN: -logKd/Ki=5.01,IC50=9.685uM
BS03 KUF A W336 M339 Y343 M469 N472 W330 M333 Y337 M459 N462 MOAD: ic50=9.685uM
PDBbind-CN: -logKd/Ki=5.01,IC50=9.685uM
BS04 KUF A I363 S374 I357 S368 MOAD: ic50=9.685uM
PDBbind-CN: -logKd/Ki=5.01,IC50=9.685uM
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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