Structure of PDB 1hn4 Chain A Binding Site BS04

Receptor Information
>1hn4 Chain A (length=129) Species: 9823 (Sus scrofa) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
GISSRALWQFRSMIKCAIPGSHPLMDFNNYGCYCGLGGSGTPVDELDRCC
ETHDNCYRDAKNLDSCKFLVDNPYTESYSYSCSNTEITCNSKNNACEAFI
CNCDRNAAICFSKAPYNKEHKNLDTKKYC
Ligand information
Ligand IDMJI
InChIInChI=1S/C22H44F3O6P/c1-3-4-5-6-7-8-9-10-11-12-13-14-15-16-17-29-18-21(31-32(26,27)28-2)19-30-20-22(23,24)25/h21H,3-20H2,1-2H3,(H,26,27)/t21-/m1/s1
InChIKeyXPTFBVFCGHXMRK-OAQYLSRUSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0CCCCCCCCCCCCCCCCOC[C@H](COCC(F)(F)F)O[P@](=O)(O)OC
ACDLabs 10.04FC(F)(F)COCC(OP(=O)(OC)O)COCCCCCCCCCCCCCCCC
OpenEye OEToolkits 1.5.0CCCCCCCCCCCCCCCCOCC(COCC(F)(F)F)OP(=O)(O)OC
CACTVS 3.341CCCCCCCCCCCCCCCCOC[CH](COCC(F)(F)F)O[P](O)(=O)OC
CACTVS 3.341CCCCCCCCCCCCCCCCOC[C@H](COCC(F)(F)F)O[P@@](O)(=O)OC
FormulaC22 H44 F3 O6 P
Name1-HEXADECYL-3-TRIFLUOROETHYL-SN-GLYCERO-2-PHOSPHATE METHANE;
MJ33 INHIBITOR
ChEMBLCHEMBL1234344
DrugBank
ZINCZINC000015546241
PDB chain1hn4 Chain A Residue 397 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB1hn4 The basis for k(cat) impairment in prophospholipase A(2) from the anion-assisted dimer structure.
Resolution1.5 Å
Binding residue
(original residue number in PDB)		S-2 L2 C29 G30 C45 H48 D49 Y52 F106
Binding residue
(residue number reindexed from 1)		S4 L7 C34 G35 C50 H53 D54 Y57 F111
Annotation score1
Binding affinityMOAD: Kd=0.15mM
PDBbind-CN: -logKd/Ki=3.82,Kd=0.15mM
Enzymatic activity
Catalytic site (original residue number in PDB) Y28 G30 G32 H48 D49 Y52 Y73 D99
Catalytic site (residue number reindexed from 1) Y33 G35 G37 H53 D54 Y57 Y78 D104
Enzyme Commision number 3.1.1.4: phospholipase A2.
Gene Ontology
Molecular Function
GO:0004623 phospholipase A2 activity
GO:0005102 signaling receptor binding
GO:0005509 calcium ion binding
GO:0005543 phospholipid binding
GO:0016787 hydrolase activity
GO:0032052 bile acid binding
GO:0046872 metal ion binding
GO:0047498 calcium-dependent phospholipase A2 activity
Biological Process
GO:0002446 neutrophil mediated immunity
GO:0006629 lipid metabolic process
GO:0006633 fatty acid biosynthetic process
GO:0006644 phospholipid metabolic process
GO:0008284 positive regulation of cell population proliferation
GO:0010524 positive regulation of calcium ion transport into cytosol
GO:0016042 lipid catabolic process
GO:0019370 leukotriene biosynthetic process
GO:0030593 neutrophil chemotaxis
GO:0032652 regulation of interleukin-1 production
GO:0032757 positive regulation of interleukin-8 production
GO:0032869 cellular response to insulin stimulus
GO:0035556 intracellular signal transduction
GO:0043406 positive regulation of MAP kinase activity
GO:0045944 positive regulation of transcription by RNA polymerase II
GO:0046324 regulation of D-glucose import
GO:0046470 phosphatidylcholine metabolic process
GO:0046471 phosphatidylglycerol metabolic process
GO:0048146 positive regulation of fibroblast proliferation
GO:0050482 arachidonate secretion
GO:0050778 positive regulation of immune response
GO:0051092 positive regulation of NF-kappaB transcription factor activity
GO:1904635 positive regulation of podocyte apoptotic process
Cellular Component
GO:0005576 extracellular region
GO:0009986 cell surface

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:1hn4, PDBe:1hn4, PDBj:1hn4
PDBsum1hn4
PubMed11560489
UniProtP00592|PA21B_PIG Phospholipase A2, major isoenzyme (Gene Name=PLA2G1B)

[Back to BioLiP]