3CS9

Human ABL kinase in complex with nilotinib

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
B	0004672	molecular_function	protein kinase activity
B	0004713	molecular_function	protein tyrosine kinase activity
B	0005524	molecular_function	ATP binding
B	0006468	biological_process	protein phosphorylation
C	0004672	molecular_function	protein kinase activity
C	0004713	molecular_function	protein tyrosine kinase activity
C	0005524	molecular_function	ATP binding
C	0006468	biological_process	protein phosphorylation
D	0004672	molecular_function	protein kinase activity
D	0004713	molecular_function	protein tyrosine kinase activity
D	0005524	molecular_function	ATP binding
D	0006468	biological_process	protein phosphorylation

Functional Information from PDB Data

site_id	AC1
Number of Residues	14
Details	BINDING SITE FOR RESIDUE NIL A 600

Chain	Residue
A	LEU248
A	MET318
A	HIS361
A	ALA380
A	ASP381
A	PHE382
A	TYR253
A	ALA269
A	LYS271
A	GLU286
A	MET290
A	ILE293
A	ILE313
A	THR315

---

site_id	AC2
Number of Residues	16
Details	BINDING SITE FOR RESIDUE NIL B 600

Chain	Residue
B	TYR253
B	ALA269
B	LYS271
B	GLU286
B	MET290
B	ILE293
B	LEU298
B	ILE313
B	THR315
B	PHE317
B	MET318
B	PHE359
B	HIS361
B	ALA380
B	ASP381
B	PHE382

---

site_id	AC3
Number of Residues	15
Details	BINDING SITE FOR RESIDUE NIL C 600

Chain	Residue
C	LEU248
C	TYR253
C	ALA269
C	LYS271
C	GLU286
C	MET290
C	LEU298
C	ILE313
C	THR315
C	PHE317
C	MET318
C	HIS361
C	ALA380
C	ASP381
C	PHE382

---

site_id	AC4
Number of Residues	14
Details	BINDING SITE FOR RESIDUE NIL D 600

Chain	Residue
D	TYR253
D	ALA269
D	LYS271
D	GLU286
D	MET290
D	LEU298
D	THR315
D	PHE317
D	MET318
D	PHE359
D	HIS361
D	ALA380
D	ASP381
D	PHE382

---

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

---

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

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10028

Chain	Residue	Details
A	ASP363
B	ASP363
C	ASP363
D	ASP363

---

site_id	SWS_FT_FI2
Number of Residues	12
Details	BINDING:

Chain	Residue	Details
B	LYS271
B	GLU316
C	LEU248
C	LYS271
C	GLU316
D	LEU248
D	LYS271
D	GLU316
A	LEU248
A	LYS271
A	GLU316
B	LEU248

---

site_id	SWS_FT_FI3
Number of Residues	4
Details	MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P42684

Chain	Residue	Details
A	SER229
B	SER229
C	SER229
D	SER229

---

site_id	SWS_FT_FI4
Number of Residues	12
Details	MOD_RES: Phosphotyrosine => ECO:0007744|PubMed:23186163

Chain	Residue	Details
B	TYR257
B	TYR413
C	TYR253
C	TYR257
C	TYR413
D	TYR253
D	TYR257
D	TYR413
A	TYR253
A	TYR257
A	TYR413
B	TYR253

---

site_id	SWS_FT_FI5
Number of Residues	4
Details	MOD_RES: Phosphotyrosine; by autocatalysis and SRC-type Tyr-kinases => ECO:0000269|PubMed:16912036

Chain	Residue	Details
A	TYR393
B	TYR393
C	TYR393
D	TYR393

---

site_id	SWS_FT_FI6
Number of Residues	4
Details	MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P00520

Chain	Residue	Details
A	SER446
B	SER446
C	SER446
D	SER446

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