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6CCF

Crystal Structure of the Human CAMKK1A in complex with Hesperadin

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 Residues14
Detailsbinding site for residue H1N A 501
ChainResidue
AILE134
AARG234
AGLY236
AASN280
ALEU282
AASP293
AVAL142
AALA155
ALYS157
AVAL212
APHE230
AASP231
ALEU232
ALEU233

site_idAC2
Number of Residues2
Detailsbinding site for residue SCN A 502
ChainResidue
AGLU199
AASN298

site_idAC3
Number of Residues15
Detailsbinding site for residue H1N B 501
ChainResidue
AARG234
BILE134
BVAL142
BALA155
BLYS157
BPHE230
BASP231
BLEU232
BLEU233
BARG234
BLYS235
BGLY236
BASN280
BLEU282
BASP293

site_idAC4
Number of Residues4
Detailsbinding site for residue EDO B 502
ChainResidue
BGLU264
BLYS332
BVAL400
BHOH641

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues24
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGKGAYGVVRlAynesedrh..........YAMK
ChainResidueDetails
AILE134-LYS157

site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IvHrDIKpsNLLL
ChainResidueDetails
AILE271-LEU283

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
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 Residues18
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

242842

PDB entries from 2025-10-08

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