Structure of PDB 5syn Chain A

Receptor sequence
>5synA (length=223) Species: 9606 (Homo sapiens) [Search protein sequence]
PLLTDAATVSGAERETAAVIFLHGLGDTGHSWADALSTIRLPHVKYICPH
APRIPVTLNMKMVMPSWFDLMGLSPDAPEDEAGIKKAAENIKALIEHEMK
NGIPANRIVLGGFSQGGALSLYTALTCPHPLAGIVALSCWLPLHRAFPQA
ANGSAKDLAILQCHGELDPMVPVRFGALTAEKLRSVVTPARVQFKTYPGV
MHSSCPQEMAAVKEFLEKLLPPV
3D structure
PDB5syn Molecular Mechanism for Isoform-Selective Inhibition of Acyl Protein Thioesterases 1 and 2 (APT1 and APT2).
ChainA
Resolution1.64 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) L33 S122 A163 D176 H210
Catalytic site (residue number reindexed from 1) L25 S114 A155 D168 H202
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 71T A L33 L78 G80 L81 P83 S122 W148 H152 M178 F183 L186 T187 L25 L70 G72 L73 P75 S114 W140 H144 M170 F175 L178 T179 MOAD: Kd=240nM
PDBbind-CN: -logKd/Ki=6.62,Kd=240nM
BindingDB: Ki=120nM,Kd=240nM,IC50=1.1e+3nM
Gene Ontology
Molecular Function
GO:0004622 lysophospholipase activity
GO:0005515 protein binding
GO:0008474 palmitoyl-(protein) hydrolase activity
GO:0016787 hydrolase activity
GO:0045296 cadherin binding
GO:0052689 carboxylic ester hydrolase activity
Biological Process
GO:0002084 protein depalmitoylation
GO:0006631 fatty acid metabolic process
GO:0007411 axon guidance
GO:0046464 acylglycerol catabolic process
GO:1905344 prostaglandin catabolic process
Cellular Component
GO:0005654 nucleoplasm
GO:0005737 cytoplasm
GO:0005795 Golgi stack
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:5syn, PDBe:5syn, PDBj:5syn
PDBsum5syn
PubMed27748579
UniProtO95372|LYPA2_HUMAN Acyl-protein thioesterase 2 (Gene Name=LYPLA2)

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