Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4QTA

Structure of human ERK2 in complex with SCH772984 revealing a novel inhibitor-induced binding pocket

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	0016020	cellular_component	membrane
A	0016301	molecular_function	kinase activity
A	0016740	molecular_function	transferase activity
A	0018107	biological_process	peptidyl-threonine phosphorylation
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	0031647	biological_process	regulation of protein stability
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	0070161	cellular_component	anchoring junction
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	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	8
Details	BINDING SITE FOR RESIDUE EDO A 401

Chain	Residue
A	ARG91
A	ALA92
A	GLN97
A	MET98
A	LYS99
A	ASP100
A	EDO407
A	HOH811

site_id	AC2
Number of Residues	8
Details	BINDING SITE FOR RESIDUE EDO A 402

Chain	Residue
A	GLY22
A	PRO23
A	ARG24
A	ILE90
A	HOH520
A	HOH582
A	HOH662
A	VAL21

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE EDO A 403

Chain	Residue
A	ARG77
A	ARG225
A	GLU326
A	ALA327

site_id	AC4
Number of Residues	7
Details	BINDING SITE FOR RESIDUE EDO A 404

Chain	Residue
A	ARG24
A	ASN47
A	ASN87
A	ASP88
A	PHE354
A	HOH536
A	HOH548

site_id	AC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE EDO A 405

Chain	Residue
A	GLY34
A	ALA35
A	HOH672
A	HOH729

site_id	AC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE EDO A 406

Chain	Residue
A	LYS138
A	PRO319
A	GLU322
A	GLU341
A	HOH770

site_id	AC7
Number of Residues	8
Details	BINDING SITE FOR RESIDUE EDO A 407

Chain	Residue
A	ASP20
A	ILE90
A	TYR102
A	EDO401
A	HOH565
A	HOH671
A	HOH776
A	HOH812

site_id	AC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE EDO A 408

Chain	Residue
A	ALA352
A	GLN355
A	PRO356
A	GLY357
A	HOH711

site_id	AC9
Number of Residues	8
Details	BINDING SITE FOR RESIDUE SO4 A 409

Chain	Residue
A	HIS61
A	GLN62
A	THR63
A	ASN123
A	HOH696
A	HOH755
A	HOH813
A	HOH833

site_id	BC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 A 410

Chain	Residue
A	ARG77
A	ARG225
A	LYS330
A	PHE331
A	HOH598
A	HOH863

site_id	BC2
Number of Residues	23
Details	BINDING SITE FOR RESIDUE 38Z A 411

Chain	Residue
A	ILE31
A	ALA35
A	TYR36
A	ALA52
A	LYS54
A	ILE56
A	TYR64
A	ARG67
A	THR68
A	GLU71
A	GLN105
A	ASP106
A	MET108
A	GLU109
A	THR110
A	LYS114
A	LEU156
A	CYS166
A	ASP167
A	HOH524
A	HOH546
A	HOH773
A	HOH781

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	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	18
Details	DNA binding: {}

Chain

Residue

Details

site_id	SWS_FT_FI2
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_FI3
Number of Residues	6
Details	Motif: {"description":"Nuclear translocation 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 autocatalysis","evidences":[{"source":"PubMed","id":"19060905","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18760948","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
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)