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5X8I

Crystal structure of human CLK1 in complex with compound 25

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
Functional Information from PDB Data
site_idAC1
Number of Residues13
Detailsbinding site for residue SQZ B 501
ChainResidue
BLEU167
BASN293
BLEU295
BASP325
BHOH795
BGLY168
BPHE172
BVAL175
BALA189
BLYS191
BPHE241
BLEU244
BGLU292

site_idAC2
Number of Residues15
Detailsbinding site for residue SQZ A 501
ChainResidue
ALEU167
AGLY168
APHE172
AVAL175
AALA189
ALYS191
APHE241
AGLU242
ALEU244
AGLU292
AASN293
ALEU295
AVAL324
AASP325
AHOH776

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues25
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGEGAFGKVVeCidhkaggrh.........VAVK
ChainResidueDetails
BLEU167-LYS191

site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. LtHtDLKpeNILF
ChainResidueDetails
BLEU284-PHE296

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
BASP288
AASP288

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
BLEU167
BLYS191
ALEU167
ALYS191

218853

PDB entries from 2024-04-24

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