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6YTI

CLK1 bound with ETH1610 (Cpd 17)

Functional Information from GO Data
ChainGOidnamespacecontents
A0004672molecular_functionprotein kinase activity
A0005524molecular_functionATP binding
A0006468biological_processprotein phosphorylation
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue EDO A 601
ChainResidue
AILE179
AGLY185
AHIS187
ATHR216

site_idAC2
Number of Residues5
Detailsbinding site for residue EDO A 602
ChainResidue
ASER205
AGLY327
AALA329
ATHR330
AGLU334

site_idAC3
Number of Residues3
Detailsbinding site for residue EDO A 603
ChainResidue
AHIS336
AGLY355
ATRP356

site_idAC4
Number of Residues3
Detailsbinding site for residue EDO A 604
ChainResidue
AHIS335
ATHR338
ATHR338

site_idAC5
Number of Residues14
Detailsbinding site for residue 7A7 A 605
ChainResidue
ALEU167
AGLU169
APHE172
AALA189
ALYS191
APHE241
AGLU242
ALEU244
ASER247
ATYR249
AASP250
AGLU292
ALEU295
AHOH701

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues25
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGEGAFGKVVeCidhkaggrh.........VAVK
ChainResidueDetails
ALEU167-LYS191

site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. LtHtDLKpeNILF
ChainResidueDetails
ALEU284-PHE296

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027
ChainResidueDetails
AASP288

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
ALYS191
ALEU167

221051

PDB entries from 2024-06-12

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