5J1W

Crystal structure of human CLK1 in complex with pyrido[3,4-g]quinazoline derivative ZW31 (compound 14)

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	5
Details	binding site for residue GOL A 501

Chain	Residue
A	PHE260
A	ARG261
A	LEU262
A	TYR373
A	HIS447

---

site_id	AC2
Number of Residues	6
Details	binding site for residue GOL A 502

Chain	Residue
A	SER483
A	HOH603
A	ASP155
A	VAL156
A	ASP478
A	LYS481

---

site_id	AC3
Number of Residues	4
Details	binding site for residue GOL A 503

Chain	Residue
A	CYS200
A	ARG204
A	GLU232
A	ILE237

---

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

Chain	Residue
A	LEU167
A	GLY245
A	SER247
A	ASP250
A	6FB506

---

site_id	AC5
Number of Residues	4
Details	binding site for residue GOL A 505

Chain	Residue
A	SER384
A	LYS408
A	TYR411
A	HOH606

---

site_id	AC6
Number of Residues	9
Details	binding site for residue 6FB A 506

Chain	Residue
A	LEU167
A	ALA189
A	LYS191
A	PHE241
A	GLU242
A	LEU244
A	GLY245
A	LEU295
A	GOL504

---

site_id	AC7
Number of Residues	6
Details	binding site for residue GOL B 501

Chain	Residue
B	LEU167
B	GLY245
B	LEU246
B	SER247
B	ASP250
B	6FB503

---

site_id	AC8
Number of Residues	7
Details	binding site for residue PO4 B 502

Chain	Residue
B	THR216
B	ASP217
B	PRO218
B	ASN219
B	THR221
C	ARG204
C	6FB506

---

site_id	AC9
Number of Residues	8
Details	binding site for residue 6FB B 503

Chain	Residue
B	LEU167
B	ALA189
B	LYS191
B	PHE241
B	GLU242
B	LEU244
B	LEU295
B	GOL501

---

site_id	AD1
Number of Residues	2
Details	binding site for residue GOL C 501

Chain	Residue
C	HIS181
C	GLY184

---

site_id	AD2
Number of Residues	4
Details	binding site for residue GOL C 502

Chain	Residue
C	LEU243
C	LEU244
C	VAL297
C	GLN298

---

site_id	AD3
Number of Residues	5
Details	binding site for residue GOL C 503

Chain	Residue
C	GLY245
C	LEU246
C	SER247
C	ASP250
C	6FB505

---

site_id	AD4
Number of Residues	5
Details	binding site for residue PO4 C 504

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

---

site_id	AD5
Number of Residues	9
Details	binding site for residue 6FB C 505

Chain	Residue
C	LEU167
C	ALA189
C	LYS191
C	PHE241
C	GLU242
C	LEU244
C	GLY245
C	LEU295
C	GOL503

---

site_id	AD6
Number of Residues	8
Details	binding site for residue 6FB C 506

Chain	Residue
B	THR216
B	PO4502
C	ASN195
C	ASP197
C	CYS200
C	GLU232
C	GLY235
C	ILE237

---

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
B	LYS191
C	LEU167
C	LYS191
A	LEU167
A	LYS191
B	LEU167

---