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5J1V

Crystal structure of human CLK1 in complex with pyrido[3,4-g]quinazoline derivative ZW29 (compound 13)

Functional Information from GO Data
ChainGOidnamespacecontents
A0004672molecular_functionprotein kinase activity
A0005524molecular_functionATP binding
A0006468biological_processprotein phosphorylation
B0004672molecular_functionprotein kinase activity
B0005524molecular_functionATP binding
B0006468biological_processprotein phosphorylation
C0004672molecular_functionprotein kinase activity
C0005524molecular_functionATP binding
C0006468biological_processprotein phosphorylation
Functional Information from PDB Data
site_idAC1
Number of Residues9
Detailsbinding site for residue 6FD A 501
ChainResidue
ALEU167
AALA189
ALYS191
APHE241
AGLU242
ALEU244
AGLY245
ALEU295
AHOH612

site_idAC2
Number of Residues2
Detailsbinding site for residue GOL A 502
ChainResidue
ASER384
ATYR411

site_idAC3
Number of Residues9
Detailsbinding site for residue 6FD B 501
ChainResidue
BLEU167
BALA189
BLYS191
BPHE241
BGLU242
BLEU244
BGLY245
BLEU295
BHOH601

site_idAC4
Number of Residues10
Detailsbinding site for residue 6FD C 501
ChainResidue
CLEU167
CALA189
CLYS191
CPHE241
CGLU242
CLEU244
CGLY245
CLEU295
CHOH603
CHOH614

site_idAC5
Number of Residues2
Detailsbinding site for residue GOL C 502
ChainResidue
CALA183
CARG186

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 Residues3
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027
ChainResidueDetails
AASP288
BASP288
CASP288

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
ALEU167
ALYS191
BLEU167
BLYS191
CLEU167
CLYS191

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PDB entries from 2025-06-11

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