5D9H

Crystal structure of SPAK (STK39) dimer in the basal activity state

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	16
Details	binding site for residue ATP A 501

Chain	Residue
A	ILE81
A	ASP204
A	LYS206
A	GLY208
A	ASN209
A	LEU211
A	ASP222
A	MG502
A	VAL89
A	ALA102
A	LYS104
A	MET150
A	LYS151
A	LEU153
A	SER157
A	ASP160

---

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

Chain	Residue
A	LYS104
A	ASN209
A	ASP222
A	ATP501

---

site_id	AC3
Number of Residues	4
Details	binding site for residue SO4 A 503

Chain	Residue
A	GLY319
A	LYS320
A	SER321
A	LYS351

---

site_id	AC4
Number of Residues	2
Details	binding site for residue SO4 A 504

Chain	Residue
A	ASN354
A	ARG355

---

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

Chain	Residue
B	ILE81
B	GLY82
B	ALA102
B	LYS104
B	LYS151
B	LEU153
B	SER157
B	LEU159
B	ASP160
B	ASP204
B	LYS206
B	GLY208
B	ASN209
B	LEU211
B	ASP222
B	MG502

---

site_id	AC6
Number of Residues	3
Details	binding site for residue MG B 502

Chain	Residue
B	ASN209
B	ASP222
B	ATP501

---

site_id	AC7
Number of Residues	3
Details	binding site for residue SO4 B 503

Chain	Residue
B	GLY319
B	LYS320
B	SER321

---

site_id	AC8
Number of Residues	2
Details	binding site for residue SO4 B 504

Chain	Residue
B	ASN354
B	ARG355

---

site_id	AC9
Number of Residues	1
Details	binding site for residue SO4 B 505

Chain	Residue
B	LYS186

---

Functional Information from PROSITE/UniProt

site_id	PS00107
Number of Residues	24
Details	PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGSGATAVVQaAlckprqer..........VAIK

Chain	Residue	Details
A	ILE81-LYS104

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159

Chain	Residue	Details
A	ASP204
B	ASP204

---

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

Chain	Residue	Details
B	ILE81
B	LYS104
A	ILE81
A	LYS104

---

site_id	SWS_FT_FI3
Number of Residues	2
Details	MOD_RES: Phosphothreonine; by WNK4 => ECO:0000269|PubMed:16382158, ECO:0000269|PubMed:16530727, ECO:0000269|PubMed:21486947

Chain	Residue	Details
B	THR243
A	THR243

---

site_id	SWS_FT_FI4
Number of Residues	2
Details	MOD_RES: Phosphothreonine => ECO:0000269|PubMed:16382158

Chain	Residue	Details
B	THR247
A	THR247

---

site_id	SWS_FT_FI5
Number of Residues	2
Details	MOD_RES: Phosphoserine; by PKC/PRKCQ => ECO:0000250|UniProtKB:Q9UEW8

Chain	Residue	Details
B	SER321
A	SER321

---

site_id	SWS_FT_FI6
Number of Residues	2
Details	MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q9UEW8

Chain	Residue	Details
B	LYS361
A	LYS361

---

site_id	SWS_FT_FI7
Number of Residues	2
Details	MOD_RES: Phosphothreonine => ECO:0000269|PubMed:21733846

Chain	Residue	Details
B	THR366
A	THR366

---

site_id	SWS_FT_FI8
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q9UEW8

Chain	Residue	Details
A	SER382
B	SER382

---

site_id	SWS_FT_FI9
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0000269|PubMed:21733846

Chain	Residue	Details
A	SER383
B	SER383

---

site_id	SWS_FT_FI10
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:21183079

Chain	Residue	Details
A	SER397
B	SER397

---