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6FYO

X-RAY STRUCTURE OF CLK1-KD(148-484)/Cpd-2 AT 2.32A

Functional Information from GO Data
ChainGOidnamespacecontents
A0004672molecular_functionprotein kinase activity
A0005524molecular_functionATP binding
A0006468biological_processprotein phosphorylation
Functional Information from PDB Data
site_idAC1
Number of Residues11
Detailsbinding site for residue EAQ A 501
ChainResidue
ALEU167
ALEU295
AASP325
AALA189
ALYS191
AGLU206
APHE241
AGLU242
ALEU244
AGLY245
ALEU246

site_idAC2
Number of Residues8
Detailsbinding site for residue SO4 A 502
ChainResidue
AARG223
ALYS267
AGLN271
ALYS274
ASER423
ASER424
AHOH617
AHOH637

site_idAC3
Number of Residues4
Detailsbinding site for residue SO4 A 503
ChainResidue
ALYS267
ASER424
AARG427
AHOH611

site_idAC4
Number of Residues4
Detailsbinding site for residue SO4 A 504
ChainResidue
AARG343
AHIS382
AHOH604
AHOH634

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 Residues1
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10027","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues9
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

246031

PDB entries from 2025-12-10

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