8EQ5

Crystal structure of the N-terminal kinase domain of RSK2 in complex with SPRED2 (131-160)

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004672	molecular_function	protein kinase activity
A	0004674	molecular_function	protein serine/threonine kinase activity
A	0005524	molecular_function	ATP binding
A	0006468	biological_process	protein phosphorylation

Functional Information from PROSITE/UniProt

site_id	PS00107
Number of Residues	27
Details	PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGQGSFGKVFlVkkisgsdarql.......YAMK

Chain	Residue	Details
A	LEU74-LYS100

---

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

Chain	Residue	Details
A	ILE189-LEU201

---

site_id	PS00284
Number of Residues	11
Details	SERPIN Serpins signature. VEVNHPFIVkL

Chain	Residue	Details
A	VAL123-LEU133

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Proton acceptor => ECO:0000250

Chain	Residue	Details
A	ASP193

---

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

Chain	Residue	Details
A	LEU74
A	LYS100

---

site_id	SWS_FT_FI3
Number of Residues	1
Details	MOD_RES: Phosphoserine; by PDPK1 => ECO:0000250|UniProtKB:P18654, ECO:0000305

Chain	Residue	Details
A	SER227

---