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1ZZL

Crystal structure of P38 with triazolopyridine

Functional Information from GO Data
ChainGOidnamespacecontents
A0000077biological_processDNA damage checkpoint signaling
A0000165biological_processMAPK cascade
A0000902biological_processcell morphogenesis
A0000922cellular_componentspindle pole
A0001502biological_processcartilage condensation
A0001525biological_processangiogenesis
A0001649biological_processosteoblast differentiation
A0001890biological_processplacenta development
A0002021biological_processresponse to dietary excess
A0002062biological_processchondrocyte differentiation
A0002862biological_processnegative regulation of inflammatory response to antigenic stimulus
A0004672molecular_functionprotein kinase activity
A0004674molecular_functionprotein serine/threonine kinase activity
A0004705molecular_functionJUN kinase activity
A0004707molecular_functionMAP kinase activity
A0004708molecular_functionMAP kinase kinase activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005576cellular_componentextracellular region
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0005829cellular_componentcytosol
A0006006biological_processglucose metabolic process
A0006355biological_processregulation of DNA-templated transcription
A0006357biological_processregulation of transcription by RNA polymerase II
A0006366biological_processtranscription 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
A0007178biological_processcell surface receptor protein serine/threonine kinase signaling pathway
A0007254biological_processJNK cascade
A0007519biological_processskeletal muscle tissue development
A0010628biological_processpositive regulation of gene expression
A0010831biological_processpositive regulation of myotube differentiation
A0016301molecular_functionkinase activity
A0016607cellular_componentnuclear speck
A0018105biological_processpeptidyl-serine phosphorylation
A0019395biological_processfatty acid oxidation
A0019899molecular_functionenzyme binding
A0019903molecular_functionprotein phosphatase binding
A0030168biological_processplatelet activation
A0030278biological_processregulation of ossification
A0030316biological_processosteoclast differentiation
A0031098biological_processstress-activated protein kinase signaling cascade
A0031281biological_processpositive regulation of cyclase activity
A0031663biological_processlipopolysaccharide-mediated signaling pathway
A0032495biological_processresponse to muramyl dipeptide
A0032496biological_processresponse to lipopolysaccharide
A0032735biological_processpositive regulation of interleukin-12 production
A0032868biological_processresponse to insulin
A0033554biological_processcellular response to stress
A0034774cellular_componentsecretory granule lumen
A0035331biological_processnegative regulation of hippo signaling
A0035556biological_processintracellular signal transduction
A0035924biological_processcellular response to vascular endothelial growth factor stimulus
A0035994biological_processresponse to muscle stretch
A0038066biological_processp38MAPK cascade
A0042307biological_processpositive regulation of protein import into nucleus
A0042770biological_processsignal transduction in response to DNA damage
A0043536biological_processpositive regulation of blood vessel endothelial cell migration
A0045648biological_processpositive regulation of erythrocyte differentiation
A0045663biological_processpositive regulation of myoblast differentiation
A0045944biological_processpositive regulation of transcription by RNA polymerase II
A0046323biological_processD-glucose import
A0046326biological_processpositive regulation of D-glucose import
A0048010biological_processvascular endothelial growth factor receptor signaling pathway
A0048273molecular_functionmitogen-activated protein kinase p38 binding
A0048863biological_processstem cell differentiation
A0051146biological_processstriated muscle cell differentiation
A0051149biological_processpositive regulation of muscle cell differentiation
A0051403biological_processstress-activated MAPK cascade
A0051525molecular_functionNFAT protein binding
A0060045biological_processpositive regulation of cardiac muscle cell proliferation
A0060348biological_processbone development
A0070935biological_process3'-UTR-mediated mRNA stabilization
A0071222biological_processcellular response to lipopolysaccharide
A0071223biological_processcellular response to lipoteichoic acid
A0071356biological_processcellular response to tumor necrosis factor
A0071479biological_processcellular response to ionizing radiation
A0071493biological_processcellular response to UV-B
A0090090biological_processnegative regulation of canonical Wnt signaling pathway
A0090336biological_processpositive regulation of brown fat cell differentiation
A0090398biological_processcellular senescence
A0090400biological_processstress-induced premature senescence
A0098586biological_processcellular response to virus
A0098978cellular_componentglutamatergic synapse
A0099179biological_processregulation of synaptic membrane adhesion
A0106310molecular_functionprotein serine kinase activity
A1900015biological_processregulation of cytokine production involved in inflammatory response
A1901741biological_processpositive regulation of myoblast fusion
A1904813cellular_componentficolin-1-rich granule lumen
A2000379biological_processpositive regulation of reactive oxygen species metabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues11
DetailsBINDING SITE FOR RESIDUE TZY A 999
ChainResidue
ATYR35
AGLY110
AHOH1127
AALA51
ALYS53
ALEU104
AVAL105
ATHR106
AHIS107
ALEU108
AMET109

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues25
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. VGSGAYGSVCaAfdtktglrv.........AVKK
ChainResidueDetails
AVAL30-LYS54

site_idPS01351
Number of Residues104
DetailsMAPK MAP kinase signature. FqsiihakrtyRElrllkhmkhenviglldvftparsleefndvylvthlmgadlnnivkcqkltddhvqfliyqilrglkyihsadiih.........RDlKpsnlavnedC
ChainResidueDetails
APHE59-CYS162

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor
ChainResidueDetails
APHE169

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING:
ChainResidueDetails
AGLY31
ALYS54

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:18691976
ChainResidueDetails
AILE17

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000269|PubMed:21444723
ChainResidueDetails
ALYS54
APRO153

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphothreonine; by MAP2K3, MAP2K4, MAP2K6 and autocatalysis => ECO:0000269|PubMed:7535770, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163
ChainResidueDetails
AGLY181

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphotyrosine; by MAP2K3, MAP2K4, MAP2K6 and autocatalysis => ECO:0000269|PubMed:7535770, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163
ChainResidueDetails
AVAL183

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:17525332
ChainResidueDetails
AGLN264

site_idSWS_FT_FI8
Number of Residues1
DetailsMOD_RES: Phosphotyrosine; by ZAP70 => ECO:0000269|PubMed:15735648
ChainResidueDetails
AASP324

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
ASER154
AASP150

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
ALYS152
AASP150

site_idCSA3
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
ALYS152
ATHR185
AASP150

site_idCSA4
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AASN155
ALYS152
AASP150

229380

PDB entries from 2024-12-25

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