2Z60

Crystal Structure of the T315I Mutant of Abl kinase bound with PPY-A

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	11
Details	BINDING SITE FOR RESIDUE P3Y A 1

Chain	Residue
A	GLY249
A	ARG367
A	LEU370
A	TYR253
A	ALA269
A	GLU316
A	PHE317
A	MET318
A	THR319
A	GLY321
A	ASN322

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Functional Information from PROSITE/UniProt

site_id	PS00107
Number of Residues	24
Details	PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGGGQYGEVYeGvwkkyslt..........VAVK

Chain	Residue	Details
A	LEU248-LYS271

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

Chain	Residue	Details
A	PHE359-VAL371

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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	ASP363

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

Chain	Residue	Details
A	GLU316
A	LEU248

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site_id	SWS_FT_FI3
Number of Residues	1
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159

Chain	Residue	Details
A	LYS271

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site_id	SWS_FT_FI4
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P42684

Chain	Residue	Details
A	SER229

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site_id	SWS_FT_FI5
Number of Residues	3
Details	MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P00519

Chain	Residue	Details
A	TYR253
A	TYR257
A	TYR413

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site_id	SWS_FT_FI6
Number of Residues	1
Details	MOD_RES: Phosphotyrosine; by autocatalysis and SRC-type Tyr-kinases => ECO:0000269|PubMed:10988075, ECO:0000269|PubMed:12748290

Chain	Residue	Details
A	TYR393

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site_id	SWS_FT_FI7
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0000269|PubMed:9109492

Chain	Residue	Details
A	SER446

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