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6YLC

Biochemical, Cellular and Structural Characterization of Novel ERK3 Inhibitors

Functional Information from GO Data
ChainGOidnamespacecontents
A0004672molecular_functionprotein kinase activity
A0004707molecular_functionMAP kinase activity
A0005524molecular_functionATP binding
A0006468biological_processprotein phosphorylation
B0004672molecular_functionprotein kinase activity
B0004707molecular_functionMAP kinase activity
B0005524molecular_functionATP binding
B0006468biological_processprotein phosphorylation
C0004672molecular_functionprotein kinase activity
C0004707molecular_functionMAP kinase activity
C0005524molecular_functionATP binding
C0006468biological_processprotein phosphorylation
D0004672molecular_functionprotein kinase activity
D0004707molecular_functionMAP kinase activity
D0005524molecular_functionATP binding
D0006468biological_processprotein phosphorylation
Functional Information from PDB Data
site_idAC1
Number of Residues13
Detailsbinding site for residue OXW A 401
ChainResidue
ALEU26
ATHR113
AASP114
APHE159
CASP164
AGLY27
ACYS28
AGLY29
AALA47
AGLN108
AGLU109
AMET111
AGLU112

site_idAC2
Number of Residues13
Detailsbinding site for residue OXW B 401
ChainResidue
BLEU26
BGLY27
BCYS28
BVAL34
BALA47
BGLN108
BGLU109
BTYR110
BMET111
BGLU112
BPHE159
BASP171
BHOH512

site_idAC3
Number of Residues11
Detailsbinding site for residue OXW C 401
ChainResidue
CLEU26
CASN31
CALA47
CLYS49
CGLN108
CGLU109
CMET111
CGLU112
CASP114
CPHE159
CASP171

site_idAC4
Number of Residues9
Detailsbinding site for residue OXW D 401
ChainResidue
DASN31
DVAL34
DLYS49
DGLU109
DTYR110
DMET111
DGLU112
DPHE159
DPHE172

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues25
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGCGGNGLVFsAvdndcdkrv.........AIKK
ChainResidueDetails
ALEU26-LYS50

site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. VlHrDLKpaNLFI
ChainResidueDetails
AVAL148-ILE160

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027
ChainResidueDetails
AASP152
BASP152
CASP152
DASP152

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
CLEU26
CLYS49
DLEU26
DLYS49
ALEU26
ALYS49
BLEU26
BLYS49

site_idSWS_FT_FI3
Number of Residues4
DetailsMOD_RES: Phosphoserine; by PAK1, PAK2 and PAK3 => ECO:0000269|PubMed:21177870, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER189
BSER189
CSER189
DSER189

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PDB entries from 2024-05-15

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