Structure of PDB 5sym Chain A

Receptor sequence
>5symA (length=223) Species: 9606 (Homo sapiens) [Search protein sequence]
TPLPAIVPAARKATAAVIFLHGLGDTGHGWAEAFAGIRSSHIKYICPHAP
VRPVTLNMNVAMPSWFDIIGLSPDSQEDESGIKQAAENIKALIDQEVKNG
IPSNRIILGGFSQGGALSLYTALTTQQKLAGVTALSCWLPLRASFPQGPI
GGANRDISILQCHGDCDPLVPLMFGSLTVEKLKTLVNPANVTFKTYEGMM
HSSCQQEMMDVKQFIDKLLPPID
3D structure
PDB5sym Molecular Mechanism for Isoform-Selective Inhibition of Acyl Protein Thioesterases 1 and 2 (APT1 and APT2).
ChainA
Resolution1.55 Å
3D
structure
Catalytic site residues are labeled in the structure
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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.
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 71Q A I75 G77 L78 S79 P80 W145 R149 L176 F181 T185 I68 G70 L71 S72 P73 W138 R142 L169 F174 T178 MOAD: Ki=280nM
PDBbind-CN: -logKd/Ki=6.55,Ki=280nM
BindingDB: Ki=300nM
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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