5B2L

A crucial role of Cys218 in the stabilization of an unprecedented auto-inhibition form of MAP2K7

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	16
Details	binding site for residue EPE A 501

Chain	Residue
A	GLU141
A	ARG233
A	MET363
A	GLY364
A	PHE365
A	SER366
A	HOH604
A	HOH646
A	GLN149
A	ARG168
A	ARG169
A	SER170
A	THR206
A	ASP207
A	PRO231
A	GLU232

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site_id	AC2
Number of Residues	5
Details	binding site for residue EPE A 502

Chain	Residue
A	THR333
A	LYS339
A	PRO357
A	LEU358
A	PRO360

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site_id	AC3
Number of Residues	3
Details	binding site for residue GOL A 503

Chain	Residue
A	GLY126
A	ASP375
A	LYS389

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Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	VAL255-LEU267

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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	ASP259

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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	LYS165
A	MET142

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site_id	SWS_FT_FI3
Number of Residues	1
Details	MOD_RES: Phosphoserine; by MAP3K => ECO:0000250

Chain	Residue	Details
A	SER287

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site_id	SWS_FT_FI4
Number of Residues	1
Details	MOD_RES: Phosphothreonine; by MAP3K => ECO:0000250

Chain	Residue	Details
A	THR291

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site_id	SWS_FT_FI5
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163

Chain	Residue	Details
A	SER427

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