3VUT

Crystal structures of non-phosphorylated MAP2K4

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 PROSITE/UniProt

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

Chain	Residue	Details
A	ILE108-LYS131

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

Chain	Residue	Details
A	ILE225-LEU237

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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, ECO:0000255|PROSITE-ProRule:PRU10027

Chain	Residue	Details
A	ASP229
B	ASP229

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

Chain	Residue	Details
A	ILE108
A	LYS131
B	ILE108
B	LYS131

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site_id	SWS_FT_FI3
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648

Chain	Residue	Details
A	SER90
B	SER90

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site_id	SWS_FT_FI4
Number of Residues	2
Details	MOD_RES: Phosphoserine; by MAP3K => ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:24275569

Chain	Residue	Details
A	SER257
B	SER257

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site_id	SWS_FT_FI5
Number of Residues	2
Details	MOD_RES: Phosphothreonine; by MAP3K => ECO:0000269|PubMed:9003778

Chain	Residue	Details
A	THR261
B	THR261

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