6FT9

Crystal structure of CLK1 in complex with inhibitor 16

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	11
Details	binding site for residue E6W A 501

Chain	Residue
A	LEU167
A	BR502
A	HOH635
A	GLU169
A	ALA189
A	PHE241
A	GLU242
A	LEU243
A	LEU244
A	GLU292
A	LEU295

---

site_id	AC2
Number of Residues	4
Details	binding site for residue BR A 502

Chain	Residue
A	SER247
A	ASP250
A	E6W501
A	HOH661

---

site_id	AC3
Number of Residues	3
Details	binding site for residue PO4 A 503

Chain	Residue
A	SER384
A	LYS410
A	TYR411

---

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

Chain	Residue
A	LEU258
A	PRO259
A	ARG311
A	HOH623
A	HOH629

---

site_id	AC5
Number of Residues	5
Details	binding site for residue GOL A 505

Chain	Residue
A	LYS434
A	GLU438
A	MET440
A	HOH651
A	HOH732

---

site_id	AC6
Number of Residues	6
Details	binding site for residue NA A 506

Chain	Residue
A	HIS344
A	TYR345
A	ARG346
A	TRP363
A	PHE379
A	HIS387

---

site_id	AC7
Number of Residues	7
Details	binding site for residue GOL A 507

Chain	Residue
A	PHE251
A	PHE260
A	ARG261
A	HIS264
A	ARG314
A	THR315
A	LEU316

---

site_id	AC8
Number of Residues	11
Details	binding site for residue E6W B 501

Chain	Residue
B	LEU167
B	GLU169
B	ALA189
B	VAL225
B	PHE241
B	GLU242
B	LEU244
B	GLU292
B	LEU295
B	BR502
B	HOH668

---

site_id	AC9
Number of Residues	3
Details	binding site for residue BR B 502

Chain	Residue
B	SER247
B	ASP250
B	E6W501

---

site_id	AD1
Number of Residues	5
Details	binding site for residue PO4 B 503

Chain	Residue
B	SER384
B	LYS408
B	LYS410
B	TYR411
B	HOH605

---

site_id	AD2
Number of Residues	6
Details	binding site for residue GOL B 504

Chain	Residue
B	ARG431
B	ALA432
B	LYS434
B	PHE439
B	HOH704
B	HOH723

---

site_id	AD3
Number of Residues	6
Details	binding site for residue NA B 505

Chain	Residue
B	HIS344
B	ARG346
B	TRP363
B	CYS367
B	PHE379
B	HIS387

---

site_id	AD4
Number of Residues	10
Details	binding site for residue E6W C 501

Chain	Residue
C	LEU167
C	GLU169
C	ALA189
C	PHE241
C	GLU242
C	LEU244
C	GLU292
C	LEU295
C	BR502
C	HOH656

---

site_id	AD5
Number of Residues	4
Details	binding site for residue BR C 502

Chain	Residue
C	SER247
C	ASP250
C	E6W501
C	HOH650

---

site_id	AD6
Number of Residues	6
Details	binding site for residue PO4 C 503

Chain	Residue
A	HIS335
A	SER337
A	THR338
C	HIS335
C	SER337
C	THR338

---

site_id	AD7
Number of Residues	5
Details	binding site for residue GOL C 504

Chain	Residue
C	SER205
C	GLY327
C	ALA329
C	THR330
C	GLU334

---

site_id	AD8
Number of Residues	7
Details	binding site for residue NA C 505

Chain	Residue
C	ARG346
C	TRP363
C	CYS367
C	PHE379
C	HIS387
C	HIS344
C	TYR345

---

Functional Information from PROSITE/UniProt

site_id	PS00107
Number of Residues	25
Details	PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGEGAFGKVVeCidhkaggrh.........VAVK

Chain	Residue	Details
A	LEU167-LYS191

---

site_id	PS00108
Number of Residues	13
Details	PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. LtHtDLKpeNILF

Chain	Residue	Details
A	LEU284-PHE296

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	3
Details	ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027

Chain	Residue	Details
A	ASP288
B	ASP288
C	ASP288

---

site_id	SWS_FT_FI2
Number of Residues	6
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159

Chain	Residue	Details
A	LEU167
A	LYS191
B	LEU167
B	LYS191
C	LEU167
C	LYS191

---