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4YNO

Crystal structure of MAPK13 at INACTIVE FORM

Replaces:  4EXU
Functional Information from GO Data
ChainGOidnamespacecontents
A0000165biological_processMAPK cascade
A0000166molecular_functionnucleotide binding
A0004672molecular_functionprotein kinase activity
A0004674molecular_functionprotein serine/threonine kinase activity
A0004707molecular_functionMAP kinase activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006468biological_processprotein phosphorylation
A0006970biological_processresponse to osmotic stress
A0007049biological_processcell cycle
A0016301molecular_functionkinase activity
A0016310biological_processphosphorylation
A0016740molecular_functiontransferase activity
A0018105biological_processpeptidyl-serine phosphorylation
A0032755biological_processpositive regulation of interleukin-6 production
A0033554biological_processcellular response to stress
A0034644biological_processcellular response to UV
A0035556biological_processintracellular signal transduction
A0050729biological_processpositive regulation of inflammatory response
A0051403biological_processstress-activated MAPK cascade
A0070301biological_processcellular response to hydrogen peroxide
A0071347biological_processcellular response to interleukin-1
A0072709biological_processcellular response to sorbitol
A0072740biological_processcellular response to anisomycin
A0106310molecular_functionprotein serine kinase activity
A1903936biological_processcellular response to sodium arsenite
Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues25
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. VGSGAYGSVCsAidkrsgekv.........AIKK
ChainResidueDetails
AVAL31-LYS55

site_idPS01351
Number of Residues103
DetailsMAPK MAP kinase signature. FqseifakrayREllllkhmqhenviglldvftpasslrnfydfylvmpfmqtdlqkimgmefseekiqylvyqmlkglkyihsagvvh..........RDlKpgnlavnedC
ChainResidueDetails
APHE60-CYS162

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
AASP150

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
ALYS54
AVAL31

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18088087
ChainResidueDetails
ASER47

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphothreonine; by MAP2K3, MAP2K4, MAP2K6 and MAP2K7 => ECO:0000269|PubMed:9374491
ChainResidueDetails
ATHR180

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphotyrosine; by MAP2K3, MAP2K4, MAP2K6 and MAP2K7 => ECO:0000269|PubMed:9374491
ChainResidueDetails
ATYR182

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:19369195
ChainResidueDetails
ASER350

218500

PDB entries from 2024-04-17

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