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6BQQ

Crystal Structure of the Human CAMKK2B in complex with BI2526

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 R78 A 501
ChainResidue
AILE171
ALYS338
AHOH659
AVAL179
AVAL249
APHE267
AGLU268
ALEU269
AVAL270
AASN271
ALEU319

site_idAC2
Number of Residues4
Detailsbinding site for residue ACT A 502
ChainResidue
ASER159
ALYS168
AASP169
AHOH644

site_idAC3
Number of Residues6
Detailsbinding site for residue ACT A 503
ChainResidue
AGLN272
AARG311
AASN335
ALEU344
ASER345
AASN346

site_idAC4
Number of Residues3
Detailsbinding site for residue ACT A 504
ChainResidue
AASP169
ATYR190
AILE365

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues24
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGKGSYGVVKlAynendnty..........YAMK
ChainResidueDetails
AILE171-LYS194

site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IiHrDIKpsNLLV
ChainResidueDetails
AILE308-VAL320

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027
ChainResidueDetails
AASP312

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
AILE171
ALYS194

219140

PDB entries from 2024-05-01

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