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6YKY

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 Residues9
Detailsbinding site for residue OWQ A 401
ChainResidue
ACYS28
AVAL34
AGLU109
AMET111
AGLU112
ATHR113
AASP114
APHE159
BALA235

site_idAC2
Number of Residues11
Detailsbinding site for residue OWQ B 401
ChainResidue
BLEU26
BCYS28
BGLY29
BVAL34
BGLN108
BGLU109
BTYR110
BMET111
BGLU112
BASN117
BPHE159

site_idAC3
Number of Residues10
Detailsbinding site for residue OWQ C 401
ChainResidue
AALA235
AGLU239
CGLY30
CVAL34
CGLN108
CGLU109
CTYR110
CMET111
CPHE159
CASP171

site_idAC4
Number of Residues11
Detailsbinding site for residue OWQ D 401
ChainResidue
DLEU26
DGLY30
DASN31
DGLN108
DGLU109
DTYR110
DMET111
DTHR113
DASP114
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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