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6FYV

X-RAY STRUCTURE OF CLK4-KD(146-480)/CX-4945 AT 2.46A

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 Residues14
Detailsbinding site for residue 3NG A 501
ChainResidue
ALEU167
ALEU295
AVAL324
AASP325
AHOH601
AHOH628
AGLY168
AGLU169
APHE172
AALA189
ALYS191
APHE241
AGLU242
ALEU244

site_idAC2
Number of Residues6
Detailsbinding site for residue SO4 A 502
ChainResidue
ASER384
ALYS410
ATYR411
ASER423
ASER424
AHOH606

site_idAC3
Number of Residues5
Detailsbinding site for residue SO4 A 503
ChainResidue
AARG343
AARG346
ASER424
AARG427
AHOH607

site_idAC4
Number of Residues4
Detailsbinding site for residue SO4 A 504
ChainResidue
ALYS283
AARG393
AARG430
AHOH629

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues25
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGEGAFGKVVeCidhgmdgmh.........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

239149

PDB entries from 2025-07-23

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