Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4FV2

Crystal Structure of the ERK2 complexed with EK5

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	0005929	cellular_component	cilium
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	0006974	biological_process	DNA damage response
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	0007507	biological_process	heart development
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	0009887	biological_process	animal organ morphogenesis
A	0010759	biological_process	positive regulation of macrophage chemotaxis
A	0010800	biological_process	positive regulation of peptidyl-threonine phosphorylation
A	0014032	biological_process	neural crest cell development
A	0014044	biological_process	Schwann cell development
A	0015630	cellular_component	microtubule cytoskeleton
A	0016301	molecular_function	kinase activity
A	0016740	molecular_function	transferase activity
A	0019858	biological_process	cytosine metabolic process
A	0019902	molecular_function	phosphatase binding
A	0030278	biological_process	regulation of ossification
A	0030641	biological_process	regulation of cellular pH
A	0030878	biological_process	thyroid gland development
A	0031143	cellular_component	pseudopodium
A	0031663	biological_process	lipopolysaccharide-mediated signaling pathway
A	0032206	biological_process	positive regulation of telomere maintenance
A	0032496	biological_process	response to lipopolysaccharide
A	0032872	biological_process	regulation of stress-activated MAPK cascade
A	0033598	biological_process	mammary gland epithelial cell proliferation
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	0036064	cellular_component	ciliary basal body
A	0038127	biological_process	ERBB signaling pathway
A	0038133	biological_process	ERBB2-ERBB3 signaling pathway
A	0042473	biological_process	outer ear morphogenesis
A	0042552	biological_process	myelination
A	0042802	molecular_function	identical protein binding
A	0043330	biological_process	response to exogenous dsRNA
A	0045202	cellular_component	synapse
A	0045542	biological_process	positive regulation of cholesterol biosynthetic process
A	0045596	biological_process	negative regulation of cell differentiation
A	0048009	biological_process	insulin-like growth factor receptor signaling pathway
A	0048538	biological_process	thymus development
A	0050852	biological_process	T cell receptor signaling pathway
A	0050853	biological_process	B cell receptor signaling pathway
A	0051403	biological_process	stress-activated MAPK cascade
A	0051493	biological_process	regulation of cytoskeleton organization
A	0060020	biological_process	Bergmann glial cell differentiation
A	0060291	biological_process	long-term synaptic potentiation
A	0060324	biological_process	face development
A	0060425	biological_process	lung morphogenesis
A	0060440	biological_process	trachea formation
A	0060716	biological_process	labyrinthine layer blood vessel development
A	0061308	biological_process	cardiac neural crest cell development involved in heart development
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	0071356	biological_process	cellular response to tumor necrosis factor
A	0072584	biological_process	caveolin-mediated endocytosis
A	0072686	cellular_component	mitotic spindle
A	0090170	biological_process	regulation of Golgi inheritance
A	0097542	cellular_component	ciliary tip
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	16
Details	BINDING SITE FOR RESIDUE EK5 A 401

Chain	Residue
A	ILE29
A	GLN103
A	ASP104
A	MET106
A	ASP109
A	LEU154
A	HOH658
A	HOH674
A	GLY30
A	GLU31
A	GLY32
A	GLY35
A	VAL37
A	ALA50
A	LYS52
A	ILE82

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 A 402

Chain	Residue
A	ARG189
A	ARG192
A	TYR231
A	HOH580
A	HOH611

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 A 403

Chain	Residue
A	THR61
A	ARG65
A	LEU168
A	ARG170
A	VAL186

site_id	AC4
Number of Residues	8
Details	BINDING SITE FOR RESIDUE GOL A 404

Chain	Residue
A	GLU79
A	ASN80
A	TYR126
A	GLN130
A	ARG133
A	ASP160
A	HOH519
A	HOH550

site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE EDO A 405

Chain	Residue
A	HIS297
A	LYS298
A	ARG299
A	GLN304
A	HOH577

site_id	AC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE EDO A 406

Chain	Residue
A	LYS149
A	SER151
A	HOH583

site_id	AC7
Number of Residues	3
Details	BINDING SITE FOR RESIDUE EDO A 407

Chain	Residue
A	LYS115
A	HIS118
A	ASN222

site_id	AC8
Number of Residues	2
Details	BINDING SITE FOR RESIDUE EDO A 408

Chain	Residue
A	PRO309
A	TYR310

site_id	AC9
Number of Residues	3
Details	BINDING SITE FOR RESIDUE EDO A 409

Chain	Residue
A	ALA280
A	SER282
A	GLU343

site_id	BC1
Number of Residues	8
Details	BINDING SITE FOR RESIDUE GOL A 410

Chain	Residue
A	ASP18
A	ARG89
A	ALA90
A	GLN95
A	MET96
A	LYS97
A	ASP98
A	HIS267

site_id	BC2
Number of Residues	1
Details	BINDING SITE FOR RESIDUE GOL A 411

Chain	Residue
A	TYR314

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	ILE29-LYS53

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

Chain	Residue	Details
A	VAL143-LEU155

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

Chain	Residue	Details
A	PHE57-CME159

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	18
Details	DNA binding: {}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	2
Details	Motif: {"description":"TXY","evidences":[{"source":"PubMed","id":"18760948","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
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_FI4
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_FI5
Number of Residues	9
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
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_FI7
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_FI8
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_FI9
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_FI10
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18760948","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI11
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)