2WU7

Crystal Structure of the Human CLK3 in complex with V25

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	16
Details	BINDING SITE FOR RESIDUE V25 A 1483

Chain	Residue
A	LEU162
A	GLU237
A	GLU287
A	ASN288
A	LEU290
A	ASP320
A	HOH2043
A	HOH2045
A	GLY163
A	GLU164
A	PHE167
A	VAL170
A	ALA184
A	LYS186
A	VAL220
A	PHE236

---

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 A 1484

Chain	Residue
A	ARG195
A	ARG199
A	LYS405
A	HOH2158

---

site_id	AC3
Number of Residues	8
Details	BINDING SITE FOR RESIDUE SO4 A 1485

Chain	Residue
A	ARG272
A	HIS275
A	THR462
A	LEU463
A	ALA464
A	HOH2159
A	HOH2160
A	HOH2161

---

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 A 1486

Chain	Residue
A	HIS330
A	THR332
A	THR333
A	HOH2162

---

site_id	AC5
Number of Residues	2
Details	BINDING SITE FOR RESIDUE SO4 A 1487

Chain	Residue
A	HIS396
A	HIS399

---

site_id	AC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 A 1488

Chain	Residue
A	VAL191
A	GLY192
A	ARG338
A	ASN379
A	HOH2163
A	HOH2164

---

site_id	AC7
Number of Residues	2
Details	BINDING SITE FOR RESIDUE CL A 1489

Chain	Residue
A	HIS330
A	HIS331

---

site_id	AC8
Number of Residues	1
Details	BINDING SITE FOR RESIDUE CL A 1490

Chain	Residue
A	ARG338

---

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	LEU162-LYS186

---

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

Chain	Residue	Details
A	LEU279-PHE291

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027

Chain	Residue	Details
A	LEU431

---

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

Chain	Residue	Details
A	SER310
A	ILE334

---

site_id	SWS_FT_FI3
Number of Residues	1
Details	MOD_RES: Phosphotyrosine => ECO:0007744|PubMed:18669648

Chain	Residue	Details
A	ARG155

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569

Chain	Residue	Details
A	GLU157

---

site_id	SWS_FT_FI5
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163

Chain	Residue	Details
A	ALA197
A	ARG199

---

site_id	SWS_FT_FI6
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:20068231

Chain	Residue	Details
A	ASN215

---

site_id	SWS_FT_FI7
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231

Chain	Residue	Details
A	ASP224
A	PHE226

---

site_id	SWS_FT_FI8
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:23186163

Chain	Residue	Details
A	ASP283

---

Catalytic Information from CSA

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

Chain	Residue	Details
A	GLU287
A	ASP283

---

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

Chain	Residue	Details
A	LYS285
A	ASP283

---

site_id	CSA3
Number of Residues	3
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
A	THR337
A	LYS285
A	ASP283

---

site_id	CSA4
Number of Residues	3
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
A	LYS285
A	ASP283
A	ASN288

---