Structure of PDB 6hgv Chain A

Receptor sequence
>6hgvA (length=319) Species: 9606 (Homo sapiens) [Search protein sequence]
PTSCNPSDMSHGYVTVKPRVRLHFVELGSGPAVCLCHGFPESWYSWRYQI
PALAQAGYRVLAMDMKGYGESSAPPEIEEYCMEVLCKEMVTFLDKLGLSQ
AVFIGHDWGGMLVWYMALFYPERVRAVASLNTPFIPANPNMSPLESIKAN
PVFDYQLYFQEPGVAEAELEQNLSRTFKSLFRASDESVLSMHKVCEAGGL
FVNSPEEPSLSRMVTEEEIQFYVQQFKKSGFRGPLNWYRNMERNWKWACK
SLGRKILIPALMVTAEKDFVLVPQMSQHMEDWIPHLKRGHIEDCGHWTQM
DKPTEVNQILIKWLDSDAR
3D structure
PDB6hgv Computer-Aided Selective Optimization of Side Activities of Talinolol.
ChainA
Resolution2.0 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 D335 W336 D496 H524
Catalytic site (residue number reindexed from 1) F39 D107 W108 D268 H296
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 MG A H506 D509 H278 D281
BS02 G3Q A D335 W336 M339 F381 Y383 Q384 M419 Y466 M469 H524 D107 W108 M111 F153 Y155 Q156 M191 Y238 M241 H296 MOAD: ic50=2.8uM
PDBbind-CN: -logKd/Ki=5.55,IC50=2.8uM
BindingDB: IC50=2800nM
Gene Ontology
Molecular Function
GO:0003824 catalytic activity

View graph for
Molecular Function
External links
PDB RCSB:6hgv, PDBe:6hgv, PDBj:6hgv
PDBsum6hgv
PubMed31223445
UniProtP34913|HYES_HUMAN Bifunctional epoxide hydrolase 2 (Gene Name=EPHX2)

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