5H2U

Crystal structure of PTK6 Kinase Domain complexed 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
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	17
Details	binding site for residue 1N1 A 501

Chain	Residue
A	LEU197
A	MET267
A	ALA268
A	GLY270
A	LEU319
A	GLY329
A	ASP330
A	HOH612
A	HOH688
A	VAL205
A	ALA217
A	ILE218
A	LYS219
A	LEU248
A	ILE262
A	THR264
A	LEU266

---

site_id	AC2
Number of Residues	7
Details	binding site for residue GOL A 502

Chain	Residue
A	ASP312
A	ARG316
A	TYR342
A	HIS345
A	TRP353
A	HOH602
A	HOH658

---

site_id	AC3
Number of Residues	5
Details	binding site for residue GOL A 503

Chain	Residue
A	ARG311
A	ALA334
A	ILE337
A	GLU339
A	TYR364

---

site_id	AC4
Number of Residues	5
Details	binding site for residue GOL A 504

Chain	Residue
A	GLU235
A	TYR308
A	ILE309
A	ARG311
A	GLY332

---

site_id	AC5
Number of Residues	16
Details	binding site for residue 1N1 B 501

Chain	Residue
B	LEU197
B	VAL205
B	ALA217
B	ILE218
B	LYS219
B	LEU248
B	ILE262
B	THR264
B	LEU266
B	MET267
B	ALA268
B	GLY270
B	GLY329
B	ASP330
B	HOH684
B	HOH703

---

site_id	AC6
Number of Residues	7
Details	binding site for residue GOL B 502

Chain	Residue
B	ASP312
B	ARG316
B	HIS345
B	TRP353
B	HOH601
B	HOH613
B	HOH622

---

site_id	AC7
Number of Residues	5
Details	binding site for residue GOL B 503

Chain	Residue
B	ARG311
B	ALA334
B	ARG335
B	TYR364
B	HOH606

---

site_id	AC8
Number of Residues	7
Details	binding site for residue GOL B 504

Chain	Residue
B	GLU235
B	TYR308
B	ILE309
B	ARG311
B	GLY332
B	ARG335
B	HOH679

---

site_id	AC9
Number of Residues	11
Details	binding site for residue 1N1 C 501

Chain	Residue
C	ALA217
C	LYS219
C	ILE262
C	THR264
C	MET267
C	ALA268
C	LYS269
C	GLY270
C	GLU274
C	ASP330
C	HOH643

---

site_id	AD1
Number of Residues	7
Details	binding site for residue GOL C 502

Chain	Residue
C	ASP312
C	ARG316
C	HIS345
C	TRP353
C	HOH605
C	HOH649
C	HOH652

---

site_id	AD2
Number of Residues	5
Details	binding site for residue GOL C 503

Chain	Residue
C	ARG311
C	ALA334
C	ILE337
C	GLU339
C	TYR364

---

site_id	AD3
Number of Residues	6
Details	binding site for residue GOL C 504

Chain	Residue
C	GLU235
C	ASN307
C	TYR308
C	ILE309
C	ARG311
C	GLY332

---

site_id	AD4
Number of Residues	9
Details	binding site for residue GOL D 501

Chain	Residue
D	ARG316
D	TYR342
D	HIS345
D	PRO350
D	TRP353
D	HOH638
D	HOH668
D	HOH694
D	ASP312

---

site_id	AD5
Number of Residues	7
Details	binding site for residue GOL D 502

Chain	Residue
D	ARG311
D	ALA334
D	ILE337
D	GLU339
D	TYR342
D	TYR364
D	HOH606

---

site_id	AD6
Number of Residues	6
Details	binding site for residue GOL D 503

Chain	Residue
D	GLU235
D	TYR308
D	ILE309
D	ARG311
D	GLY332
D	ARG335

---

site_id	AD7
Number of Residues	14
Details	binding site for residue 1N1 D 504

Chain	Residue
D	LEU197
D	VAL205
D	ALA217
D	LYS219
D	LEU248
D	ILE262
D	THR264
D	MET267
D	ALA268
D	GLY270
D	ASP330
D	HOH656
D	HOH685
D	HOH705

---

site_id	AD8
Number of Residues	13
Details	binding site for Di-peptide CXM B 184 and GLU B 185

Chain	Residue
B	ARG186
B	LYS240
B	TYR251
B	ALA252
B	VAL253
B	VAL254
B	SER255
B	HOH609
B	HOH624
B	HOH646
B	HOH674
D	LEU410
D	GLU411

---

site_id	AD9
Number of Residues	9
Details	binding site for Di-peptide CXM C 184 and GLU C 185

Chain	Residue
A	GLU411
C	ARG186
C	LYS240
C	TYR251
C	ALA252
C	VAL253
C	SER255
C	HOH620
C	HOH678

---

site_id	AE1
Number of Residues	11
Details	binding site for Di-peptide CXM D 184 and GLU D 185

Chain	Residue
D	ARG186
D	LYS240
D	TYR251
D	ALA252
D	VAL253
D	VAL254
D	SER255
D	HOH617
D	HOH658
D	HOH669
D	HOH698

---

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	LEU197-LYS219

---

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

Chain	Residue	Details
A	TYR308-VAL320

---

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	ASP312
B	ASP312
C	ASP312
D	ASP312

---

site_id	SWS_FT_FI2
Number of Residues	4
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159

Chain	Residue	Details
A	LEU197
B	LEU197
C	LEU197
D	LEU197

---

site_id	SWS_FT_FI3
Number of Residues	4
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000305|PubMed:27480927, ECO:0000305|PubMed:27993680

Chain	Residue	Details
A	LYS219
B	LYS219
C	LYS219
D	LYS219

---

site_id	SWS_FT_FI4
Number of Residues	8
Details	MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:12121988

Chain	Residue	Details
A	TYR342
A	TYR351
B	TYR342
B	TYR351
C	TYR342
C	TYR351
D	TYR342
D	TYR351

---