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6BQL

Crystal Structure of the Human CAMKK2B in complex with TAE-226

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 Residues16
Detailsbinding site for residue BI9 A 501
ChainResidue
AILE171
AASN317
ALEU319
APHE337
ALYS338
AHOH605
AHOH608
AHOH666
AGLY172
ATYR176
AALA192
AGLU268
ALEU269
AVAL270
AASN271
AGLY273

site_idAC2
Number of Residues3
Detailsbinding site for residue EDO A 502
ChainResidue
AGLN235
AASN335
AGLU336

site_idAC3
Number of Residues2
Detailsbinding site for residue CL A 503
ChainResidue
APRO315
ASER316

site_idAC4
Number of Residues4
Detailsbinding site for residue ACT A 504
ChainResidue
ASER175
ATYR176
AGLN204
AGLN232

site_idAC5
Number of Residues5
Detailsbinding site for residue ACT A 505
ChainResidue
AASP169
AGLU170
ALYS338
AASP341
AHOH706

site_idAC6
Number of Residues2
Detailsbinding site for residue NH4 A 506
ChainResidue
AGLU236
AASP330

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

222624

PDB entries from 2024-07-17

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