2ZV9

Lyn Tyrosine Kinase Domain-PP2 complex

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004672	molecular_function	protein kinase activity
A	0004713	molecular_function	protein tyrosine kinase activity
A	0005524	molecular_function	ATP binding
A	0006468	biological_process	protein phosphorylation

Functional Information from PDB Data

site_id	AC1
Number of Residues	10
Details	BINDING SITE FOR RESIDUE PP2 A 513

Chain	Residue
A	LEU253
A	LEU374
A	ALA273
A	GLU290
A	MET294
A	ILE317
A	THR319
A	GLU320
A	MET322
A	SER326

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Functional Information from PROSITE/UniProt

site_id	PS00107
Number of Residues	23
Details	PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGAGQFGEVWmGyynnstk...........VAVK

Chain	Residue	Details
A	LEU253-LYS275

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site_id	PS00109
Number of Residues	13
Details	PROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. YIHrDLRAANVLV

Chain	Residue	Details
A	TYR363-VAL375

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10028

Chain	Residue	Details
A	ASP367

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site_id	SWS_FT_FI2
Number of Residues	2
Details	BINDING: BINDING => ECO:0000305

Chain	Residue	Details
A	LEU253
A	LYS275

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site_id	SWS_FT_FI3
Number of Residues	4
Details	MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P07948

Chain	Residue	Details
A	TYR306
A	TYR316
A	TYR460
A	TYR473

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site_id	SWS_FT_FI4
Number of Residues	1
Details	MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:10415030, ECO:0000269|PubMed:16272347, ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079

Chain	Residue	Details
A	TYR397

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site_id	SWS_FT_FI5
Number of Residues	1
Details	MOD_RES: Phosphotyrosine; by autocatalysis, CSK and MATK => ECO:0000269|PubMed:10415030, ECO:0007744|PubMed:18034455, ECO:0007744|PubMed:19144319

Chain	Residue	Details
A	TYR508

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