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3FLN

P38 kinase crystal structure in complex with R1487

Functional Information from GO Data
ChainGOidnamespacecontents
C0000077biological_processDNA damage checkpoint signaling
C0000165biological_processMAPK cascade
C0000902biological_processcell morphogenesis
C0000922cellular_componentspindle pole
C0001502biological_processcartilage condensation
C0001525biological_processangiogenesis
C0001649biological_processosteoblast differentiation
C0001890biological_processplacenta development
C0002021biological_processresponse to dietary excess
C0002062biological_processchondrocyte differentiation
C0002862biological_processnegative regulation of inflammatory response to antigenic stimulus
C0004672molecular_functionprotein kinase activity
C0004674molecular_functionprotein serine/threonine kinase activity
C0004707molecular_functionMAP kinase activity
C0004708molecular_functionMAP kinase kinase activity
C0005515molecular_functionprotein binding
C0005524molecular_functionATP binding
C0005576cellular_componentextracellular region
C0005634cellular_componentnucleus
C0005654cellular_componentnucleoplasm
C0005737cellular_componentcytoplasm
C0005739cellular_componentmitochondrion
C0005829cellular_componentcytosol
C0006006biological_processglucose metabolic process
C0006355biological_processregulation of DNA-templated transcription
C0006357biological_processregulation of transcription by RNA polymerase II
C0006366biological_processtranscription by RNA polymerase II
C0006468biological_processprotein phosphorylation
C0006915biological_processapoptotic process
C0006935biological_processchemotaxis
C0006974biological_processDNA damage response
C0007165biological_processsignal transduction
C0007166biological_processcell surface receptor signaling pathway
C0007178biological_processcell surface receptor protein serine/threonine kinase signaling pathway
C0007519biological_processskeletal muscle tissue development
C0010628biological_processpositive regulation of gene expression
C0010831biological_processpositive regulation of myotube differentiation
C0016301molecular_functionkinase activity
C0016607cellular_componentnuclear speck
C0018105biological_processpeptidyl-serine phosphorylation
C0019395biological_processfatty acid oxidation
C0019899molecular_functionenzyme binding
C0019903molecular_functionprotein phosphatase binding
C0030168biological_processplatelet activation
C0030278biological_processregulation of ossification
C0030316biological_processosteoclast differentiation
C0031098biological_processstress-activated protein kinase signaling cascade
C0031281biological_processpositive regulation of cyclase activity
C0031663biological_processlipopolysaccharide-mediated signaling pathway
C0032495biological_processresponse to muramyl dipeptide
C0032496biological_processresponse to lipopolysaccharide
C0032735biological_processpositive regulation of interleukin-12 production
C0032868biological_processresponse to insulin
C0034774cellular_componentsecretory granule lumen
C0035331biological_processnegative regulation of hippo signaling
C0035556biological_processintracellular signal transduction
C0035924biological_processcellular response to vascular endothelial growth factor stimulus
C0035994biological_processresponse to muscle stretch
C0038066biological_processp38MAPK cascade
C0042307biological_processpositive regulation of protein import into nucleus
C0042770biological_processsignal transduction in response to DNA damage
C0043536biological_processpositive regulation of blood vessel endothelial cell migration
C0045648biological_processpositive regulation of erythrocyte differentiation
C0045663biological_processpositive regulation of myoblast differentiation
C0045944biological_processpositive regulation of transcription by RNA polymerase II
C0046323biological_processglucose import
C0046326biological_processpositive regulation of glucose import
C0048010biological_processvascular endothelial growth factor receptor signaling pathway
C0048273molecular_functionmitogen-activated protein kinase p38 binding
C0048863biological_processstem cell differentiation
C0051146biological_processstriated muscle cell differentiation
C0051149biological_processpositive regulation of muscle cell differentiation
C0051403biological_processstress-activated MAPK cascade
C0051525molecular_functionNFAT protein binding
C0060045biological_processpositive regulation of cardiac muscle cell proliferation
C0060348biological_processbone development
C0070935biological_process3'-UTR-mediated mRNA stabilization
C0071222biological_processcellular response to lipopolysaccharide
C0071223biological_processcellular response to lipoteichoic acid
C0071356biological_processcellular response to tumor necrosis factor
C0071479biological_processcellular response to ionizing radiation
C0071493biological_processcellular response to UV-B
C0090090biological_processnegative regulation of canonical Wnt signaling pathway
C0090336biological_processpositive regulation of brown fat cell differentiation
C0090398biological_processcellular senescence
C0090400biological_processstress-induced premature senescence
C0098586biological_processcellular response to virus
C0098978cellular_componentglutamatergic synapse
C0099179biological_processregulation of synaptic membrane adhesion
C0106310molecular_functionprotein serine kinase activity
C1900015biological_processregulation of cytokine production involved in inflammatory response
C1901741biological_processpositive regulation of myoblast fusion
C1904813cellular_componentficolin-1-rich granule lumen
C2000379biological_processpositive regulation of reactive oxygen species metabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues15
DetailsBINDING SITE FOR RESIDUE 3FN C 361
ChainResidue
CGLY33
CMET109
CALA111
CASP112
CASN115
CHOH381
CHOH464
CVAL38
CALA51
CLYS53
CLEU86
CLEU104
CVAL105
CTHR106
CHIS107

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues25
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. VGSGAYGSVCaAfdtktglrv.........AVKK
ChainResidueDetails
CVAL30-LYS54

site_idPS01351
Number of Residues104
DetailsMAPK MAP kinase signature. FqsiihakrtyRElrllkhmkhenviglldvftparsleefndvylvthlmgadlnnivkcqkltddhvqfliyqilrglkyihsadiih.........RDlKpsnlavnedC
ChainResidueDetails
CPHE59-CYS162

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor
ChainResidueDetails
CASP168

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING:
ChainResidueDetails
CVAL30
CLYS53

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163
ChainResidueDetails
CSER2

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:18691976
ChainResidueDetails
CTHR16

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000269|PubMed:21444723
ChainResidueDetails
CLYS53
CLYS152

site_idSWS_FT_FI6
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
CTHR180

site_idSWS_FT_FI7
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
CTYR182

site_idSWS_FT_FI8
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:17525332
ChainResidueDetails
CTHR263

site_idSWS_FT_FI9
Number of Residues1
DetailsMOD_RES: Phosphotyrosine; by ZAP70 => ECO:0000269|PubMed:15735648
ChainResidueDetails
CTYR323

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
CSER154
CASP150

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
CLYS152
CASP150

site_idCSA3
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
CLYS152
CTHR185
CASP150

site_idCSA4
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
CASN155
CLYS152
CASP150

222624

PDB entries from 2024-07-17

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