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4HGT

Crystal structure of ck1d with 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
Functional Information from PDB Data
site_idAC1
Number of Residues17
DetailsBINDING SITE FOR RESIDUE 15G A 301
ChainResidue
AILE15
ALEU85
AILE148
AASP149
AHOH436
AHOH574
BGLU2
BARG10
BLEU11
AGLY18
AILE23
ALEU25
AALA36
ALYS38
APRO66
AMET82
AGLU83

site_idAC2
Number of Residues21
DetailsBINDING SITE FOR RESIDUE 15G B 301
ChainResidue
ATHR27
AGLY32
AHOH476
BARG13
BILE15
BILE23
BALA36
BLYS38
BPRO66
BMET82
BGLU83
BLEU84
BLEU85
BGLY86
BLEU135
BILE148
BASP149
BHOH452
BHOH525
BHOH560
BHOH619

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues24
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGSGSFGDIYlGtdiaagee..........VAIK
ChainResidueDetails
AILE15-LYS38

site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. FiHrDVKpdNFLM
ChainResidueDetails
APHE124-MET136

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
AASP128
BASP128

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
AILE15
ALYS38
BILE15
BLYS38

218853

PDB entries from 2024-04-24

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