1OPK

Structural basis for the auto-inhibition of c-Abl tyrosine kinase

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004672	molecular_function	protein 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	3
Details	BINDING SITE FOR RESIDUE MYR A 1

Chain	Residue
A	LEU360
A	GLU481
A	LEU529

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site_id	AC2
Number of Residues	15
Details	BINDING SITE FOR RESIDUE P16 A 2

Chain	Residue
A	ILE332
A	THR334
A	GLU335
A	MET337
A	GLY340
A	LEU389
A	ALA399
A	ASP400
A	HOH791
A	TYR272
A	VAL275
A	ALA288
A	LYS290
A	GLU305
A	MET309

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site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL A 3

Chain	Residue
A	TYR339
A	TYR345
A	GLY391
A	GLU392
A	ASN393
A	HIS394

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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	LEU267-LYS290

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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	ASN382

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

Chain	Residue	Details
A	LEU267
A	GLU335

---

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

Chain	Residue	Details
A	LYS290

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site_id	SWS_FT_FI4
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P00519

Chain	Residue	Details
A	SER69

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site_id	SWS_FT_FI5
Number of Residues	1
Details	MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000250|UniProtKB:P00519

Chain	Residue	Details
A	TYR89

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site_id	SWS_FT_FI6
Number of Residues	8
Details	MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P00519

Chain	Residue	Details
A	TYR134
A	TYR147
A	TYR158
A	TYR191
A	TYR204
A	TYR272
A	TYR276
A	TYR432

---

site_id	SWS_FT_FI7
Number of Residues	1
Details	MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P42684

Chain	Residue	Details
A	TYR234

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site_id	SWS_FT_FI8
Number of Residues	1
Details	MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:12748290

Chain	Residue	Details
A	TYR245

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site_id	SWS_FT_FI9
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_FI10
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	TYR412

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site_id	SWS_FT_FI11
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0000269|PubMed:9109492

Chain	Residue	Details
A	SER465

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Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
A	ARG386
A	ASN382

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