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

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	Active site: {"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	9
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI3
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine; by PDPK1","evidences":[{"source":"UniProtKB","id":"P18654","evidenceCode":"ECO:0000250"},{"evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

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