1OPL

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
B	0004672	molecular_function	protein kinase activity
B	0005524	molecular_function	ATP binding
B	0006468	biological_process	protein phosphorylation

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MYR A 538

Chain	Residue
A	LEU360
A	GLU481
A	ILE521
A	LEU529

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site_id	AC2
Number of Residues	15
Details	BINDING SITE FOR RESIDUE P16 A 539

Chain	Residue
A	MET309
A	ILE332
A	THR334
A	GLU335
A	MET337
A	GLY340
A	LEU389
A	ALA399
A	ASP400
A	PHE401
A	TYR272
A	VAL275
A	ALA288
A	LYS290
A	GLU305

---

site_id	AC3
Number of Residues	10
Details	BINDING SITE FOR RESIDUE P16 B 538

Chain	Residue
B	TYR272
B	GLU305
B	MET309
B	THR334
B	GLU335
B	MET337
B	GLY340
B	LEU389
B	ALA399
B	PHE401

---

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	2
Details	ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10028

Chain	Residue	Details
A	ASN382
B	ASN382

---

site_id	SWS_FT_FI2
Number of Residues	6
Details	BINDING:

Chain	Residue	Details
A	LEU267
A	LYS290
A	GLU335
B	LEU267
B	LYS290
B	GLU335

---

site_id	SWS_FT_FI3
Number of Residues	2
Details	SITE: Breakpoint for translocation to form BCR-ABL and NUP214-ABL1 fusion proteins => ECO:0000269|PubMed:15361874, ECO:0000269|PubMed:3021337

Chain	Residue	Details
A	HIS45
B	HIS45

---

site_id	SWS_FT_FI4
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0000269|PubMed:16543148, ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19690332

Chain	Residue	Details
A	SER69
B	SER69

---

site_id	SWS_FT_FI5
Number of Residues	2
Details	MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:16912036, ECO:0000269|PubMed:18775435

Chain	Residue	Details
A	TYR89
B	TYR89

---

site_id	SWS_FT_FI6
Number of Residues	12
Details	MOD_RES: Phosphotyrosine => ECO:0000269|PubMed:16912036

Chain	Residue	Details
A	TYR134
B	TYR191
B	TYR204
B	TYR234
A	TYR147
A	TYR158
A	TYR191
A	TYR204
A	TYR234
B	TYR134
B	TYR147
B	TYR158

---

site_id	SWS_FT_FI7
Number of Residues	2
Details	MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:16912036

Chain	Residue	Details
A	TYR245
B	TYR245

---

site_id	SWS_FT_FI8
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P42684

Chain	Residue	Details
A	SER248
B	SER248

---

site_id	SWS_FT_FI9
Number of Residues	6
Details	MOD_RES: Phosphotyrosine => ECO:0007744|PubMed:23186163

Chain	Residue	Details
A	TYR272
A	TYR276
A	TYR432
B	TYR272
B	TYR276
B	TYR432

---

site_id	SWS_FT_FI10
Number of Residues	2
Details	MOD_RES: Phosphotyrosine; by autocatalysis and SRC-type Tyr-kinases => ECO:0000269|PubMed:16912036

Chain	Residue	Details
A	TYR412
B	TYR412

---

site_id	SWS_FT_FI11
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P00520

Chain	Residue	Details
A	SER465
B	SER465

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