Structure of PDB 5kre Chain A

Receptor sequence
>5kreA (length=224) Species: 9606 (Homo sapiens) [Search protein sequence]
VLQRCIVSPAGRHSASLIFLHGSGDSGQGLRMWIKQVLNQDLTFQHIKII
YPTAPPRSYTPMKGGISNVWFDRFKITNDCPEHLESIDVMCQVLTDLIDE
EVKSGIKKNRILIGGFSMGGCMAMHLAYRNHQDVAGVFALSSFLNKASAV
YQALQKSNGVLPELFQCHGTADELVLHSWAEETNSMLKSLGVTTKFHSFP
NVYHELSKTELDILKLWILTKLPG
3D structure
PDB5kre Discovery of a Selective Covalent Inhibitor of Lysophospholipase-like 1 (LYPLAL1) as a Tool to Evaluate the Role of this Serine Hydrolase in Metabolism.
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) S30 S124 N165 D179 H211
Catalytic site (residue number reindexed from 1) S23 S117 N158 D172 H204
Enzyme Commision number 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 6WG A S30 Y66 R80 I83 S124 M125 L181 V182 S23 Y59 R73 I76 S117 M118 L174 V175 PDBbind-CN: -logKd/Ki=7.23,IC50=0.059uM
Gene Ontology
Molecular Function
GO:0004622 lysophospholipase activity
GO:0005515 protein binding
GO:0008474 palmitoyl-(protein) hydrolase activity
GO:0016298 lipase activity
GO:0016787 hydrolase activity
GO:0016788 hydrolase activity, acting on ester bonds
GO:0052689 carboxylic ester hydrolase activity
Biological Process
GO:0008150 biological_process
GO:0098734 macromolecule depalmitoylation
GO:0160049 negative regulation of cGAS/STING signaling pathway
Cellular Component
GO:0005737 cytoplasm
GO:0005739 mitochondrion
GO:0005829 cytosol

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:5kre, PDBe:5kre, PDBj:5kre
PDBsum5kre
PubMed27391855
UniProtQ5VWZ2|LYPL1_HUMAN Lysophospholipase-like protein 1 (Gene Name=LYPLAL1)

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