5DBX

Crystal structure of murine SPAK(T243D) in complex with AMPPNP

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	13
Details	binding site for residue ANP A 401

Chain	Residue
A	GLY84
A	LEU211
A	MG402
A	HOH502
A	HOH510
A	ALA85
A	THR86
A	ALA87
A	VAL89
A	LYS104
A	MET150
A	LYS151
A	LEU153

---

site_id	AC2
Number of Residues	1
Details	binding site for residue MG A 402

Chain	Residue
A	ANP401

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site_id	AC3
Number of Residues	10
Details	binding site for residue ANP B 401

Chain	Residue
B	ILE81
B	GLY84
B	ALA85
B	ALA87
B	VAL89
B	LYS104
B	LYS151
B	LEU153
B	MG402
B	HOH502

---

site_id	AC4
Number of Residues	2
Details	binding site for residue MG B 402

Chain	Residue
B	ASN209
B	ANP401

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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

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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
A	ILE81
A	LYS104
B	ILE81
B	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
A	ASP243
B	ASP243

---

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

Chain	Residue	Details
A	THR247
B	THR247

---

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

Chain	Residue	Details
A	SER321
B	SER321

---

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

Chain	Residue	Details
A	LYS361
B	LYS361

---

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

Chain	Residue	Details
A	THR366
B	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

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