Structure of PDB 5sym Chain A Binding Site BS01

Receptor Information
>5sym Chain A (length=223) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
TPLPAIVPAARKATAAVIFLHGLGDTGHGWAEAFAGIRSSHIKYICPHAP
VRPVTLNMNVAMPSWFDIIGLSPDSQEDESGIKQAAENIKALIDQEVKNG
IPSNRIILGGFSQGGALSLYTALTTQQKLAGVTALSCWLPLRASFPQGPI
GGANRDISILQCHGDCDPLVPLMFGSLTVEKLKTLVNPANVTFKTYEGMM
HSSCQQEMMDVKQFIDKLLPPID
Ligand information
Ligand ID71Q
InChIInChI=1S/C18H17ClF3N3O3/c19-13-4-3-12(18(20,21)22)10-14(13)23-16(26)11-24-5-7-25(8-6-24)17(27)15-2-1-9-28-15/h1-4,9-10H,5-8,11H2,(H,23,26)
InChIKeyOXKNHBBDOIMFFQ-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 12.01N1(CCN(CC1)C(c2ccco2)=O)CC(=O)Nc3cc(C(F)(F)F)ccc3Cl
OpenEye OEToolkits 2.0.5c1cc(oc1)C(=O)N2CCN(CC2)CC(=O)Nc3cc(ccc3Cl)C(F)(F)F
CACTVS 3.385FC(F)(F)c1ccc(Cl)c(NC(=O)CN2CCN(CC2)C(=O)c3occc3)c1
FormulaC18 H17 Cl F3 N3 O3
NameN-[2-chloro-5-(trifluoromethyl)phenyl]-2-[4-(furan-2-carbonyl)piperazin-1-yl]acetamide
ChEMBLCHEMBL600764
DrugBank
ZINCZINC000053193522
PDB chain5sym Chain A Residue 301 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB5sym Molecular Mechanism for Isoform-Selective Inhibition of Acyl Protein Thioesterases 1 and 2 (APT1 and APT2).
Resolution1.55 Å
Binding residue
(original residue number in PDB)		I75 G77 L78 S79 P80 W145 R149 L176 F181 T185
Binding residue
(residue number reindexed from 1)		I68 G70 L71 S72 P73 W138 R142 L169 F174 T178
Annotation score1
Binding affinityMOAD: Ki=280nM
PDBbind-CN: -logKd/Ki=6.55,Ki=280nM
BindingDB: Ki=300nM
Enzymatic activity
Catalytic site (original residue number in PDB) L30 S119 N161 D174 H208
Catalytic site (residue number reindexed from 1) L23 S112 N154 D167 H201
Enzyme Commision number 3.1.2.-
3.1.2.22: palmitoyl-protein hydrolase.
Gene Ontology
Molecular Function
GO:0004620 phospholipase activity
GO:0004622 lysophospholipase activity
GO:0005515 protein binding
GO:0008474 palmitoyl-(protein) hydrolase activity
GO:0016298 lipase activity
GO:0016787 hydrolase activity
GO:0052689 carboxylic ester hydrolase activity
Biological Process
GO:0002084 protein depalmitoylation
GO:0006631 fatty acid metabolic process
GO:0015908 fatty acid transport
GO:0042997 negative regulation of Golgi to plasma membrane protein transport
GO:1905336 negative regulation of aggrephagy
Cellular Component
GO:0005634 nucleus
GO:0005654 nucleoplasm
GO:0005737 cytoplasm
GO:0005739 mitochondrion
GO:0005783 endoplasmic reticulum
GO:0005829 cytosol
GO:0005886 plasma membrane
GO:0031965 nuclear membrane
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:5sym, PDBe:5sym, PDBj:5sym
PDBsum5sym
PubMed27748579
UniProtO75608|LYPA1_HUMAN Acyl-protein thioesterase 1 (Gene Name=LYPLA1)

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