6PBC

Structural basis for the activation of PLC-gamma isozymes by phosphorylation and cancer-associated mutations

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004435	molecular_function	phosphatidylinositol phospholipase C activity
A	0005509	molecular_function	calcium ion binding
A	0006629	biological_process	lipid metabolic process
A	0007165	biological_process	signal transduction
A	0008081	molecular_function	phosphoric diester hydrolase activity
A	0009395	biological_process	phospholipid catabolic process
A	0035556	biological_process	intracellular signal transduction

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	binding site for residue CA A 1301

Chain	Residue
A	ASN336
A	GLU365
A	ASP367
A	GLU414
A	HOH1553

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site_id	AC2
Number of Residues	5
Details	binding site for residue NA A 1302

Chain	Residue
A	ARG100
A	TYR93
A	GLN94
A	ASP96
A	PHE99

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Functional Information from PROSITE/UniProt

site_id	PS00018
Number of Residues	13
Details	EF_HAND_1 EF-hand calcium-binding domain. DRNREDRISakDL

Chain	Residue	Details
A	ASP165-LEU177

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	5
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00448

Chain	Residue	Details
A	ASP165
A	ASN167
A	GLU169
A	ARG171
A	ASP176

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site_id	SWS_FT_FI2
Number of Residues	1
Details	MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:Q62077

Chain	Residue	Details
A	TYR977

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