6FYK

X-Ray structure of CLK2-KD(136-496)/Indazole1 at 2.39A

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	13
Details	binding site for residue EAZ A 501

Chain	Residue
A	GLU171
A	LEU297
A	ASP327
A	HOH607
A	HOH688
A	PHE174
A	ALA191
A	LYS193
A	PHE243
A	GLU244
A	LEU246
A	GLU294
A	ASN295

---

site_id	AC2
Number of Residues	14
Details	binding site for residue EAZ B 501

Chain	Residue
B	PHE174
B	ALA191
B	LYS193
B	VAL227
B	PHE243
B	GLU244
B	LEU246
B	GLU294
B	ASN295
B	LEU297
B	VAL326
B	ASP327
B	HOH685
B	HOH711

---

site_id	AC3
Number of Residues	16
Details	binding site for residue EAZ C 501

Chain	Residue
C	GLU171
C	PHE174
C	VAL177
C	ALA191
C	LYS193
C	VAL227
C	PHE243
C	GLU244
C	LEU246
C	GLU294
C	ASN295
C	LEU297
C	VAL326
C	ASP327
C	HOH679
C	HOH680

---

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	LEU169-LYS193

---

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

Chain	Residue	Details
A	LEU286-PHE298

---

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	ASP290
B	ASP290
C	ASP290

---

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

Chain	Residue	Details
B	LYS193
C	LEU169
C	LYS193
A	LEU169
A	LYS193
B	LEU169

---

site_id	SWS_FT_FI3
Number of Residues	3
Details	MOD_RES: Phosphoserine; by autocatalysis => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:23186163

Chain	Residue	Details
A	SER142
B	SER142
C	SER142

---

site_id	SWS_FT_FI4
Number of Residues	3
Details	MOD_RES: Phosphotyrosine => ECO:0007744|PubMed:19369195

Chain	Residue	Details
A	TYR153
B	TYR153
C	TYR153

---

site_id	SWS_FT_FI5
Number of Residues	3
Details	MOD_RES: Phosphothreonine; by PKB/AKT2 => ECO:0000250|UniProtKB:O35491

Chain	Residue	Details
A	THR344
B	THR344
C	THR344

---