6BJE

Crystal Structure of Lysophospholipase A2 Conjugated with Phenylmethylsulfonyl Fluoride

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0002084	biological_process	protein depalmitoylation
A	0004622	molecular_function	lysophospholipase activity
A	0005515	molecular_function	protein binding
A	0005654	cellular_component	nucleoplasm
A	0005737	cellular_component	cytoplasm
A	0005795	cellular_component	Golgi stack
A	0005829	cellular_component	cytosol
A	0006631	biological_process	fatty acid metabolic process
A	0007411	biological_process	axon guidance
A	0008474	molecular_function	palmitoyl-(protein) hydrolase activity
A	0016787	molecular_function	hydrolase activity
A	0045296	molecular_function	cadherin binding
A	0046464	biological_process	acylglycerol catabolic process
A	0052689	molecular_function	carboxylic ester hydrolase activity
A	0070062	cellular_component	extracellular exosome
A	1905344	biological_process	prostaglandin catabolic process
B	0002084	biological_process	protein depalmitoylation
B	0004622	molecular_function	lysophospholipase activity
B	0005515	molecular_function	protein binding
B	0005654	cellular_component	nucleoplasm
B	0005737	cellular_component	cytoplasm
B	0005795	cellular_component	Golgi stack
B	0005829	cellular_component	cytosol
B	0006631	biological_process	fatty acid metabolic process
B	0007411	biological_process	axon guidance
B	0008474	molecular_function	palmitoyl-(protein) hydrolase activity
B	0016787	molecular_function	hydrolase activity
B	0045296	molecular_function	cadherin binding
B	0046464	biological_process	acylglycerol catabolic process
B	0052689	molecular_function	carboxylic ester hydrolase activity
B	0070062	cellular_component	extracellular exosome
B	1905344	biological_process	prostaglandin catabolic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	8
Details	binding site for residue PMS A 301

Chain	Residue
A	LEU33
A	LEU78
A	SER122
A	GLN123
A	TRP148
A	MET178
A	HIS210
B	ASN67

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site_id	AC2
Number of Residues	15
Details	binding site for Di-peptide PMS B 301 and SER B 122

Chain	Residue
B	LEU66
B	LEU78
B	PHE121
B	GLN123
B	GLY124
B	GLY125
B	ALA126
B	LEU145
B	SER146
B	CYS147
B	TRP148
B	MET178
B	VAL179
B	HIS210
B	LEU33

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: Charge relay system => ECO:0000305|PubMed:28826475

Chain	Residue	Details
A	SER122
B	SER122

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site_id	SWS_FT_FI2
Number of Residues	4
Details	ACT_SITE: Charge relay system => ECO:0000250|UniProtKB:O75608

Chain	Residue	Details
A	ASP176
A	HIS210
B	ASP176
B	HIS210

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site_id	SWS_FT_FI3
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q9QYL8

Chain	Residue	Details
A	SER82
B	SER82

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