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6G33

Crystal structure of CLK1 in complex with 5-iodotubercidin

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 Residues15
Detailsbinding site for residue 5ID A 501
ChainResidue
AGLY168
ALEU295
AIOD502
AHOH603
AHOH620
AHOH628
AHOH673
APHE172
AVAL175
AALA189
APHE241
AGLU242
ALEU244
AASP250
AGLU292

site_idAC2
Number of Residues3
Detailsbinding site for residue IOD A 502
ChainResidue
ALYS191
A5ID501
AHOH652

site_idAC3
Number of Residues2
Detailsbinding site for residue PO4 A 503
ChainResidue
AHIS335
ATHR338

site_idAC4
Number of Residues15
Detailsbinding site for residue 5ID B 501
ChainResidue
BGLY168
BPHE172
BVAL175
BALA189
BPHE241
BGLU242
BLEU244
BASP250
BGLU292
BLEU295
BIOD502
BHOH602
BHOH609
BHOH640
BHOH647

site_idAC5
Number of Residues2
Detailsbinding site for residue IOD B 502
ChainResidue
BLYS191
B5ID501

site_idAC6
Number of Residues14
Detailsbinding site for residue 5ID C 501
ChainResidue
CGLY168
CPHE172
CVAL175
CALA189
CPHE241
CGLU242
CLEU244
CASP250
CGLU292
CLEU295
CIOD502
CHOH607
CHOH620
CHOH654

site_idAC7
Number of Residues3
Detailsbinding site for residue IOD C 502
ChainResidue
CLYS191
C5ID501
CHOH624

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues25
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGEGAFGKVVeCidhkaggrh.........VAVK
ChainResidueDetails
ALEU167-LYS191
BLEU167-LYS191

site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. LtHtDLKpeNILF
ChainResidueDetails
ALEU284-PHE296
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
CASP288

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
BLEU167
BLYS191
CLEU167
CLYS191

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PDB entries from 2024-07-10

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