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3UZP

crystal structure of ck1d with PF670462 from P21 crystal form

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 Residues11
DetailsBINDING SITE FOR RESIDUE 0CK A 295
ChainResidue
AILE23
AHOH367
AHOH445
AALA36
AMET80
AMET82
AGLU83
ALEU84
ALEU85
AILE148
AHOH313

site_idAC2
Number of Residues16
DetailsBINDING SITE FOR RESIDUE 0CK B 295
ChainResidue
BILE23
BALA36
BLYS38
BILE68
BMET80
BMET82
BGLU83
BLEU84
BLEU85
BSER88
BASP91
BLEU135
BILE148
BHOH371
BHOH372
BHOH401

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
BILE15
BLYS38
AILE15
ALYS38

221051

PDB entries from 2024-06-12

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