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5AX3

Crystal structure of ERK2 complexed with allosteric and ATP-competitive inhibitors.

Functional Information from GO Data
ChainGOidnamespacecontents
A0000165biological_processMAPK cascade
A0001784molecular_functionphosphotyrosine residue binding
A0003677molecular_functionDNA binding
A0004672molecular_functionprotein kinase activity
A0004674molecular_functionprotein serine/threonine kinase activity
A0004707molecular_functionMAP kinase activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005576cellular_componentextracellular region
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0005769cellular_componentearly endosome
A0005770cellular_componentlate endosome
A0005788cellular_componentendoplasmic reticulum lumen
A0005794cellular_componentGolgi apparatus
A0005813cellular_componentcentrosome
A0005819cellular_componentspindle
A0005829cellular_componentcytosol
A0005856cellular_componentcytoskeleton
A0005886cellular_componentplasma membrane
A0005901cellular_componentcaveola
A0005925cellular_componentfocal adhesion
A0006357biological_processregulation of transcription by RNA polymerase II
A0006468biological_processprotein phosphorylation
A0006915biological_processapoptotic process
A0006935biological_processchemotaxis
A0006974biological_processDNA damage response
A0007165biological_processsignal transduction
A0007166biological_processcell surface receptor signaling pathway
A0007268biological_processchemical synaptic transmission
A0007507biological_processheart development
A0007611biological_processlearning or memory
A0008286biological_processinsulin receptor signaling pathway
A0008353molecular_functionRNA polymerase II CTD heptapeptide repeat kinase activity
A0009887biological_processanimal organ morphogenesis
A0010759biological_processpositive regulation of macrophage chemotaxis
A0010800biological_processpositive regulation of peptidyl-threonine phosphorylation
A0014032biological_processneural crest cell development
A0014044biological_processSchwann cell development
A0016020cellular_componentmembrane
A0016301molecular_functionkinase activity
A0016310biological_processphosphorylation
A0018105biological_processpeptidyl-serine phosphorylation
A0018107biological_processpeptidyl-threonine phosphorylation
A0019858biological_processcytosine metabolic process
A0019902molecular_functionphosphatase binding
A0030278biological_processregulation of ossification
A0030521biological_processandrogen receptor signaling pathway
A0030641biological_processregulation of cellular pH
A0030878biological_processthyroid gland development
A0031143cellular_componentpseudopodium
A0031647biological_processregulation of protein stability
A0031663biological_processlipopolysaccharide-mediated signaling pathway
A0032206biological_processpositive regulation of telomere maintenance
A0032496biological_processresponse to lipopolysaccharide
A0032872biological_processregulation of stress-activated MAPK cascade
A0033554biological_processcellular response to stress
A0033598biological_processmammary gland epithelial cell proliferation
A0034198biological_processcellular response to amino acid starvation
A0035094biological_processresponse to nicotine
A0035556biological_processintracellular signal transduction
A0035578cellular_componentazurophil granule lumen
A0038127biological_processERBB signaling pathway
A0038133biological_processERBB2-ERBB3 signaling pathway
A0042473biological_processouter ear morphogenesis
A0042552biological_processmyelination
A0042802molecular_functionidentical protein binding
A0043330biological_processresponse to exogenous dsRNA
A0043401biological_processsteroid hormone receptor signaling pathway
A0045202cellular_componentsynapse
A0045542biological_processpositive regulation of cholesterol biosynthetic process
A0045596biological_processnegative regulation of cell differentiation
A0048009biological_processinsulin-like growth factor receptor signaling pathway
A0048538biological_processthymus development
A0050847biological_processprogesterone receptor signaling pathway
A0050852biological_processT cell receptor signaling pathway
A0050853biological_processB cell receptor signaling pathway
A0051403biological_processstress-activated MAPK cascade
A0051493biological_processregulation of cytoskeleton organization
A0060020biological_processBergmann glial cell differentiation
A0060291biological_processlong-term synaptic potentiation
A0060324biological_processface development
A0060425biological_processlung morphogenesis
A0060440biological_processtrachea formation
A0060716biological_processlabyrinthine layer blood vessel development
A0061308biological_processcardiac neural crest cell development involved in heart development
A0070161cellular_componentanchoring junction
A0070371biological_processERK1 and ERK2 cascade
A0070849biological_processresponse to epidermal growth factor
A0071356biological_processcellular response to tumor necrosis factor
A0072584biological_processcaveolin-mediated endocytosis
A0072686cellular_componentmitotic spindle
A0090170biological_processregulation of Golgi inheritance
A0106310molecular_functionprotein serine kinase activity
A0120041biological_processpositive regulation of macrophage proliferation
A1904813cellular_componentficolin-1-rich granule lumen
A2000641biological_processregulation of early endosome to late endosome transport
Functional Information from PDB Data
site_idAC1
Number of Residues11
Detailsbinding site for residue 5ID A 401
ChainResidue
AILE22
ALEU147
BGLU360
AGLU24
AALA43
AASP97
ALEU98
AMET99
AASP102
ALYS105
ASER144

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues25
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGEGAYGMVCsAydnvnkvrv.........AIKK
ChainResidueDetails
AILE22-LYS46

site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. VlHrDLKpsNLLL
ChainResidueDetails
AVAL136-LEU148

site_idPS01351
Number of Residues103
DetailsMAPK MAP kinase signature. FehqtycqrtlREikillrfrheniigindiiraptieqmkdvyivqdlmetdlykllktqhlsndhicyflyqilrglkyihsanvlh..........RDlKpsnlllnttC
ChainResidueDetails
APHE50-CYS152

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues18
DetailsDNA_BIND:
ChainResidueDetails
ALYS249-ARG267

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027
ChainResidueDetails
AASP140

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
AILE22
ALYS45

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: N-acetylalanine => ECO:0000269|PubMed:12665801, ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378
ChainResidueDetails
AALA-7

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphoserine; by SGK1 => ECO:0000269|PubMed:19447520
ChainResidueDetails
ASER20

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphothreonine; by MAP2K1 and MAP2K2 => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163
ChainResidueDetails
ATHR176

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: Phosphotyrosine; by MAP2K1 and MAP2K2 => ECO:0000269|PubMed:19053285, ECO:0000269|PubMed:19494114, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163
ChainResidueDetails
ATYR178

site_idSWS_FT_FI8
Number of Residues1
DetailsMOD_RES: Phosphothreonine; by autocatalysis => ECO:0000269|PubMed:19060905
ChainResidueDetails
ATHR181

site_idSWS_FT_FI9
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:18760948
ChainResidueDetails
ASER236
ASER238

site_idSWS_FT_FI10
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:19369195
ChainResidueDetails
ASER274

226707

PDB entries from 2024-10-30

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