Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6SLG

HUMAN ERK2 WITH ERK1/2 INHIBITOR, AZD0364.

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000165	biological_process	MAPK cascade
A	0000166	molecular_function	nucleotide binding
A	0001784	molecular_function	phosphotyrosine residue binding
A	0003677	molecular_function	DNA binding
A	0004672	molecular_function	protein kinase activity
A	0004674	molecular_function	protein serine/threonine kinase activity
A	0004707	molecular_function	MAP kinase activity
A	0005515	molecular_function	protein binding
A	0005524	molecular_function	ATP binding
A	0005576	cellular_component	extracellular region
A	0005634	cellular_component	nucleus
A	0005654	cellular_component	nucleoplasm
A	0005737	cellular_component	cytoplasm
A	0005739	cellular_component	mitochondrion
A	0005769	cellular_component	early endosome
A	0005770	cellular_component	late endosome
A	0005788	cellular_component	endoplasmic reticulum lumen
A	0005794	cellular_component	Golgi apparatus
A	0005813	cellular_component	centrosome
A	0005819	cellular_component	spindle
A	0005829	cellular_component	cytosol
A	0005856	cellular_component	cytoskeleton
A	0005886	cellular_component	plasma membrane
A	0005901	cellular_component	caveola
A	0005925	cellular_component	focal adhesion
A	0006357	biological_process	regulation of transcription by RNA polymerase II
A	0006468	biological_process	protein phosphorylation
A	0006915	biological_process	apoptotic process
A	0006935	biological_process	chemotaxis
A	0007165	biological_process	signal transduction
A	0007166	biological_process	cell surface receptor signaling pathway
A	0007173	biological_process	epidermal growth factor receptor signaling pathway
A	0007268	biological_process	chemical synaptic transmission
A	0007611	biological_process	learning or memory
A	0008286	biological_process	insulin receptor signaling pathway
A	0008353	molecular_function	RNA polymerase II CTD heptapeptide repeat kinase activity
A	0010759	biological_process	positive regulation of macrophage chemotaxis
A	0010800	biological_process	positive regulation of peptidyl-threonine phosphorylation
A	0014044	biological_process	Schwann cell development
A	0016301	molecular_function	kinase activity
A	0016740	molecular_function	transferase activity
A	0019902	molecular_function	phosphatase binding
A	0031143	cellular_component	pseudopodium
A	0032206	biological_process	positive regulation of telomere maintenance
A	0032872	biological_process	regulation of stress-activated MAPK cascade
A	0034198	biological_process	cellular response to amino acid starvation
A	0035094	biological_process	response to nicotine
A	0035556	biological_process	intracellular signal transduction
A	0035578	cellular_component	azurophil granule lumen
A	0038127	biological_process	ERBB signaling pathway
A	0038133	biological_process	ERBB2-ERBB3 signaling pathway
A	0042552	biological_process	myelination
A	0042802	molecular_function	identical protein binding
A	0045202	cellular_component	synapse
A	0045542	biological_process	positive regulation of cholesterol biosynthetic process
A	0048009	biological_process	insulin-like growth factor receptor signaling pathway
A	0051403	biological_process	stress-activated MAPK cascade
A	0051493	biological_process	regulation of cytoskeleton organization
A	0061514	biological_process	interleukin-34-mediated signaling pathway
A	0070098	biological_process	chemokine-mediated signaling pathway
A	0070371	biological_process	ERK1 and ERK2 cascade
A	0070849	biological_process	response to epidermal growth factor
A	0072584	biological_process	caveolin-mediated endocytosis
A	0072686	cellular_component	mitotic spindle
A	0090170	biological_process	regulation of Golgi inheritance
A	0106310	molecular_function	protein serine kinase activity
A	0120041	biological_process	positive regulation of macrophage proliferation
A	0150078	biological_process	positive regulation of neuroinflammatory response
A	1904813	cellular_component	ficolin-1-rich granule lumen
A	2000641	biological_process	regulation of early endosome to late endosome transport

Functional Information from PDB Data

site_id	AC1
Number of Residues	19
Details	binding site for residue LHZ A 401

Chain	Residue
A	GLY32
A	GLN105
A	ASP106
A	MET108
A	GLU109
A	THR110
A	ASP111
A	LYS114
A	LEU156
A	ASP167
A	HOH520
A	GLU33
A	GLY34
A	TYR36
A	GLY37
A	MET38
A	VAL39
A	ALA52
A	LYS54

site_id	AC2
Number of Residues	7
Details	binding site for residue SO4 A 402

Chain	Residue
A	TYR187
A	ARG191
A	ARG194
A	TYR233
A	HOH521
A	HOH566
A	HOH567

site_id	AC3
Number of Residues	5
Details	binding site for residue SO4 A 403

Chain	Residue
A	PHE183
A	ASN257
A	LEU258
A	LYS259
A	HOH654

site_id	AC4
Number of Residues	5
Details	binding site for residue EDO A 404

Chain	Residue
A	GLN97
A	SER246
A	LEU267
A	PRO268
A	HOH526

site_id	AC5
Number of Residues	5
Details	binding site for residue EDO A 405

Chain	Residue
A	ARG77
A	TYR139
A	ALA325
A	GLU326
A	ALA327

site_id	AC6
Number of Residues	6
Details	binding site for residue EDO A 406

Chain	Residue
A	ARG91
A	ALA92
A	MET98
A	LYS99
A	ASP100
A	HIS269

site_id	AC7
Number of Residues	1
Details	binding site for residue EDO A 407

Chain	Residue
A	TYR317

Functional Information from PROSITE/UniProt

site_id	PS00107
Number of Residues	25
Details	PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGEGAYGMVCsAydnlnkvrv.........AIKK

Chain	Residue	Details
A	ILE31-LYS55

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

Chain	Residue	Details
A	VAL145-LEU157

site_id	PS01351
Number of Residues	103
Details	MAPK MAP kinase signature. FehqtycqrtlREikillrfrheniigindiiraptieqmkdvyivqdlmetdlykllktqhlsndhicyflyqilrglkyihsanvlh..........RDlKpsnlllnttC

Chain	Residue	Details
A	PHE59-CYS161

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	288
Details	Domain: {"description":"Protein kinase","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	18
Details	DNA binding: {}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	2
Details	Motif: {"description":"TXY","evidences":[{"source":"PubMed","id":"18760948","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	4
Details	Motif: {"description":"Cytoplasmic retention motif","evidences":[{"source":"PubMed","id":"18760948","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	1
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10027","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	9
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine; by SGK1","evidences":[{"source":"PubMed","id":"19447520","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	1
Details	Modified residue: {"description":"Phosphothreonine; by MAP2K1 and MAP2K2","evidences":[{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"21406692","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	1
Details	Modified residue: {"description":"Phosphotyrosine; by MAP2K1 and MAP2K2","evidences":[{"source":"PubMed","id":"19053285","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19494114","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"21406692","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	1
Details	Modified residue: {"description":"Phosphothreonine; by autocatalysis","evidences":[{"source":"PubMed","id":"19060905","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18760948","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI12
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"19369195","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)