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2G01

Pyrazoloquinolones as Novel, Selective JNK1 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
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 501
ChainResidue
AARG189
AARG192
BTHR255

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 601
ChainResidue
AARG69
AARG72
AARG150
AARG174

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 B 701
ChainResidue
BARG192
ATHR255
BARG189

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 B 801
ChainResidue
BLYS68
BARG69
BARG72
BARG150
BARG174

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE 73Q A 901
ChainResidue
AILE32
AALA53
AMET108
AMET111
AALA113
AASN114
ALEU168

site_idAC6
Number of Residues8
DetailsBINDING SITE FOR RESIDUE 73Q B 1001
ChainResidue
BMET108
BLEU110
BMET111
BASP112
BALA113
BASN114
BVAL158
BLEU168

Functional Information from PROSITE/UniProt
site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IiHrDLKpsNIVV
ChainResidueDetails
AILE147-VAL159

site_idPS01351
Number of Residues103
DetailsMAPK MAP kinase signature. FqnqthakrayRElvlmkcvnhkniigllnvftpqksleefqdvyivmelmdanlcqviqmeldhermsyllyqmlcgikhlhsagiih..........RDlKpsnivvksdC
ChainResidueDetails
APHE61-CYS163

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027
ChainResidueDetails
AASP151
BASP151

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
AILE32
ALYS55
BILE32
BLYS55

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: S-nitrosocysteine => ECO:0000250|UniProtKB:P49185
ChainResidueDetails
ACYS116
BCYS116

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphothreonine; by MAP2K7 => ECO:0000269|PubMed:11062067
ChainResidueDetails
AGLU183
BGLU183

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphotyrosine; by MAP2K4 => ECO:0000269|PubMed:11062067
ChainResidueDetails
AGLU185
BGLU185

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
ASER155
AASP151

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BSER155
BASP151

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AASP151
ALYS153

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BASP151
BLYS153

site_idCSA5
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AASP151
ATHR188
ALYS153

site_idCSA6
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BASP151
BTHR188
BLYS153

site_idCSA7
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AASN156
AASP151
ALYS153

site_idCSA8
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BASN156
BASP151
BLYS153

229183

PDB entries from 2024-12-18

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