2OIQ

Crystal Structure of chicken c-Src kinase domain in complex with the cancer drug imatinib.

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	16
Details	BINDING SITE FOR RESIDUE STI A 1001

Chain	Residue
A	VAL281
A	VAL383
A	HIS384
A	ARG385
A	ALA403
A	ASP404
A	PHE405
A	HOH1027
A	ALA293
A	LYS295
A	GLU310
A	MET314
A	ILE336
A	THR338
A	TYR340
A	MET341

---

site_id	AC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL A 1002

Chain	Residue
A	GLU517
A	ASP518
A	HOH1057
A	HOH1129
B	LYS427
B	PRO464
B	GLY465

---

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL A 1003

Chain	Residue
A	LYS427
A	PRO464
A	GLY465
B	GLU517
B	ASP518
B	HOH571

---

Functional Information from PROSITE/UniProt

site_id	PS00107
Number of Residues	23
Details	PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGQGCFGEVWmGtwngttr...........VAIK

Chain	Residue	Details
A	LEU273-LYS295

---

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

Chain	Residue	Details
A	TYR382-VAL394

---

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	LEU387
B	LEU387

---

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

Chain	Residue	Details
A	GLY274
B	GLY274

---

site_id	SWS_FT_FI3
Number of Residues	2
Details	BINDING:

Chain	Residue	Details
A	THR296
B	THR296

---

site_id	SWS_FT_FI4
Number of Residues	2
Details	MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:6273838, ECO:0000269|PubMed:8856081

Chain	Residue	Details
A	THR417
B	THR417

---

site_id	SWS_FT_FI5
Number of Residues	2
Details	MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:8856081

Chain	Residue	Details
A	GLY437
B	GLY437

---

site_id	SWS_FT_FI6
Number of Residues	2
Details	MOD_RES: S-nitrosocysteine => ECO:0000269|PubMed:19948721

Chain	Residue	Details
A	TRP499
B	TRP499

---

site_id	SWS_FT_FI7
Number of Residues	2
Details	MOD_RES: Phosphotyrosine; by CSK => ECO:0000269|PubMed:2420005

Chain	Residue	Details
A	GLN528
B	GLN528

---

Catalytic Information from CSA

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

Chain	Residue	Details
A	ASP386
A	ALA390

---

site_id	CSA2
Number of Residues	2
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
B	ASP386
B	ALA390

---

site_id	CSA3
Number of Residues	2
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
A	ARG388
A	ASP386

---

site_id	CSA4
Number of Residues	2
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
B	ARG388
B	ASP386

---

site_id	CSA5
Number of Residues	3
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
A	ARG388
A	ASN391
A	ASP386

---

site_id	CSA6
Number of Residues	3
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
B	ARG388
B	ASN391
B	ASP386

---