6CJH

Co-crystal structure of MNK2 in complex with an inhibitor

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	4
Details	binding site for residue ZN A 401

Chain	Residue
A	ARG298
A	CYS299
A	CYS311
A	CYS314

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site_id	AC2
Number of Residues	2
Details	binding site for residue ET8 A 402

Chain	Residue
A	LEU90
A	ASP226

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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. LGEGAHARVQtCinlitsqe..........YAVK

Chain	Residue	Details
A	LEU90-LYS113

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

Chain	Residue	Details
A	ILE201-CYS213

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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	ASP205

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

Chain	Residue	Details
A	LEU90
A	LYS113

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site_id	SWS_FT_FI3
Number of Residues	1
Details	BINDING:

Chain	Residue	Details
A	GLU160

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site_id	SWS_FT_FI4
Number of Residues	1
Details	BINDING: BINDING => ECO:0000269|PubMed:16917500

Chain	Residue	Details
A	GLU209

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site_id	SWS_FT_FI5
Number of Residues	3
Details	BINDING: BINDING => ECO:0000269|PubMed:16216586, ECO:0000269|PubMed:16917500

Chain	Residue	Details
A	CYS299
A	CYS311
A	CYS314

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site_id	SWS_FT_FI6
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q8CDB0

Chain	Residue	Details
A	SER74

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site_id	SWS_FT_FI7
Number of Residues	3
Details	MOD_RES: Phosphothreonine => ECO:0000269|PubMed:11463832

Chain	Residue	Details
A	THR244
A	THR249
A	THR379

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