4XLI

Crystal structure of Abl2/Arg kinase in complex with dasatinib

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	13
Details	binding site for residue 1N1 A 601

Chain	Residue
A	LEU294
A	PRO365
A	GLY367
A	LEU416
A	ALA426
A	ALA315
A	LYS317
A	GLU332
A	ILE359
A	THR361
A	GLU362
A	TYR363
A	MET364

---

site_id	AC2
Number of Residues	4
Details	binding site for residue ZN A 602

Chain	Residue
A	GLU398
A	HIS536
B	GLU398
B	HIS536

---

site_id	AC3
Number of Residues	12
Details	binding site for residue 1N1 B 600

Chain	Residue
B	ALA315
B	GLU332
B	MET336
B	VAL345
B	ILE359
B	THR361
B	GLU362
B	TYR363
B	MET364
B	PRO365
B	GLY367
B	ALA426

---

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	LEU294-LYS317

---

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

Chain	Residue	Details
A	PHE405-VAL417

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: Proton acceptor => ECO:0000250|UniProtKB:P28523, ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10028

Chain	Residue	Details
A	ASP409
B	ASP409

---

site_id	SWS_FT_FI2
Number of Residues	2
Details	BINDING: BINDING => ECO:0000250|UniProtKB:P28523, ECO:0000255|PROSITE-ProRule:PRU00159

Chain	Residue	Details
A	LEU294
B	LEU294

---

site_id	SWS_FT_FI3
Number of Residues	2
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:12748290

Chain	Residue	Details
A	LYS317
B	LYS317

---

site_id	SWS_FT_FI4
Number of Residues	2
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159

Chain	Residue	Details
A	GLU362
B	GLU362

---

site_id	SWS_FT_FI5
Number of Residues	6
Details	MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P00519

Chain	Residue	Details
A	TYR459
B	TYR299
B	TYR303
B	TYR459
A	TYR299
A	TYR303

---

site_id	SWS_FT_FI6
Number of Residues	2
Details	MOD_RES: Phosphotyrosine; by autocatalysis and SRC-type Tyr-kinases => ECO:0000250|UniProtKB:P42684

Chain	Residue	Details
A	TYR439
B	TYR439

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