6XRG

Abl 1b isoform inactive2 state

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 PROSITE/UniProt

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

Chain	Residue	Details
A	LEU267-LYS290

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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	PHE378-VAL390

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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	ASP382

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site_id	SWS_FT_FI2
Number of Residues	3
Details	BINDING:

Chain	Residue	Details
A	LEU267
A	LYS290
A	GLU335

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site_id	SWS_FT_FI3
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P42684

Chain	Residue	Details
A	SER248

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site_id	SWS_FT_FI4
Number of Residues	3
Details	MOD_RES: Phosphotyrosine => ECO:0007744|PubMed:23186163

Chain	Residue	Details
A	TYR272
A	TYR276
A	TYR432

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site_id	SWS_FT_FI5
Number of Residues	1
Details	MOD_RES: Phosphotyrosine; by autocatalysis and SRC-type Tyr-kinases => ECO:0000269|PubMed:16912036

Chain	Residue	Details
A	TYR412

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site_id	SWS_FT_FI6
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P00520

Chain	Residue	Details
A	SER465

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