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5U7R

Identification of A New Class of Potent Cdc7 Inhibitors Designed by Putative Pharmacophore Model: Synthesis and Biological Evaluation of 2,3-Dihydrothieno[3,2-d]pyrimidin-4(1H)-ones

Functional Information from GO Data
ChainGOidnamespacecontents
A0004672molecular_functionprotein kinase activity
A0004674molecular_functionprotein serine/threonine kinase activity
A0005524molecular_functionATP binding
A0006468biological_processprotein phosphorylation
B0004672molecular_functionprotein kinase activity
B0004674molecular_functionprotein serine/threonine kinase activity
B0005524molecular_functionATP binding
B0006468biological_processprotein phosphorylation
C0004672molecular_functionprotein kinase activity
C0004674molecular_functionprotein serine/threonine kinase activity
C0005524molecular_functionATP binding
C0006468biological_processprotein phosphorylation
D0004672molecular_functionprotein kinase activity
D0004674molecular_functionprotein serine/threonine kinase activity
D0005524molecular_functionATP binding
D0006468biological_processprotein phosphorylation
Functional Information from PDB Data
site_idAC1
Number of Residues9
Detailsbinding site for residue 81G A 500
ChainResidue
AILE98
AALA119
ALYS121
AGLU170
AMET172
AASP218
ALEU221
AASP232
APHE384

site_idAC2
Number of Residues10
Detailsbinding site for residue 81G B 500
ChainResidue
BILE98
BGLY101
BALA119
BLYS121
BGLU170
BMET172
BASP218
BLEU221
BASP232
BPHE384

site_idAC3
Number of Residues12
Detailsbinding site for residue 81G C 500
ChainResidue
CALA119
CLYS121
CGLU140
CMET169
CGLU170
CTYR171
CMET172
CASP218
CLEU221
CALA231
CASP232
CPHE384

site_idAC4
Number of Residues11
Detailsbinding site for residue 81G D 500
ChainResidue
DILE98
DALA119
DLYS121
DGLU140
DMET169
DGLU170
DTYR171
DMET172
DASP218
DLEU221
DPHE384

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues24
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGRGAFGEVQlVrhkasqkv..........YAMK
ChainResidueDetails
AILE98-LYS121

site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. LiHrDVKpdNMLL
ChainResidueDetails
ALEU210-LEU222

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
AASP214
BASP214
CASP214
DASP214

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
AILE98
ALYS121
BILE98
BLYS121
CILE98
CLYS121
DILE98
DLYS121

site_idSWS_FT_FI3
Number of Residues4
DetailsMOD_RES: Phosphothreonine; by ROCK2 => ECO:0000250|UniProtKB:Q62868
ChainResidueDetails
ATHR414
BTHR414
CTHR414
DTHR414

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PDB entries from 2024-08-07

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