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6UNA

Crystal structure of inactive p38gamma

Functional Information from GO Data
ChainGOidnamespacecontents
A0000165biological_processMAPK cascade
A0000287molecular_functionmagnesium ion binding
A0004672molecular_functionprotein kinase activity
A0004674molecular_functionprotein serine/threonine kinase activity
A0004707molecular_functionMAP kinase activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0005829cellular_componentcytosol
A0006468biological_processprotein phosphorylation
A0007165biological_processsignal transduction
A0007517biological_processmuscle organ development
A0010952biological_processpositive regulation of peptidase activity
A0016310biological_processphosphorylation
A0018105biological_processpeptidyl-serine phosphorylation
A0033554biological_processcellular response to stress
A0035556biological_processintracellular signal transduction
A0042770biological_processsignal transduction in response to DNA damage
A0045445biological_processmyoblast differentiation
A0045786biological_processnegative regulation of cell cycle
A0046872molecular_functionmetal ion binding
A0051149biological_processpositive regulation of muscle cell differentiation
A0051726biological_processregulation of cell cycle
A0106310molecular_functionprotein serine kinase activity
B0000165biological_processMAPK cascade
B0000287molecular_functionmagnesium ion binding
B0004672molecular_functionprotein kinase activity
B0004674molecular_functionprotein serine/threonine kinase activity
B0004707molecular_functionMAP kinase activity
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0005634cellular_componentnucleus
B0005654cellular_componentnucleoplasm
B0005737cellular_componentcytoplasm
B0005739cellular_componentmitochondrion
B0005829cellular_componentcytosol
B0006468biological_processprotein phosphorylation
B0007165biological_processsignal transduction
B0007517biological_processmuscle organ development
B0010952biological_processpositive regulation of peptidase activity
B0016310biological_processphosphorylation
B0018105biological_processpeptidyl-serine phosphorylation
B0033554biological_processcellular response to stress
B0035556biological_processintracellular signal transduction
B0042770biological_processsignal transduction in response to DNA damage
B0045445biological_processmyoblast differentiation
B0045786biological_processnegative regulation of cell cycle
B0046872molecular_functionmetal ion binding
B0051149biological_processpositive regulation of muscle cell differentiation
B0051726biological_processregulation of cell cycle
B0106310molecular_functionprotein serine kinase activity
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue GOL A 401
ChainResidue
AGLY126
AGLU127
AASP128
AARG129

site_idAC2
Number of Residues5
Detailsbinding site for residue SO4 A 402
ChainResidue
ALEU119
AGLU123
AASN162
ACYS165
BGLU312

site_idAC3
Number of Residues4
Detailsbinding site for residue GOL B 401
ChainResidue
BGLY126
BGLU127
BASP128
BARG129

site_idAC4
Number of Residues6
Detailsbinding site for residue SO4 B 402
ChainResidue
BLEU119
BGLU123
BARG129
BASN162
BGLU163
BCYS165

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues25
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. VGSGAYGAVCsAvdgrtgakv.........AIKK
ChainResidueDetails
AVAL33-LYS57

site_idPS01351
Number of Residues104
DetailsMAPK MAP kinase signature. FqselfakrayRElrllkhmrhenviglldvftpdetlddftdfylvmpfmgtdlgklmkheklgedriqflvyqmlkglryihaagiih.........RDlKpgnlavnedC
ChainResidueDetails
APHE62-CYS165

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
AASP153
BASP153

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
AVAL33
ALYS56
BVAL33
BLYS56

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Phosphothreonine; by MAP2K3 and MAP2K6 => ECO:0000250|UniProtKB:Q63538
ChainResidueDetails
ATHR183
BTHR183

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ATYR185
BTYR185

224004

PDB entries from 2024-08-21

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