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6BRC

Crystal Structure of the Human CAMKK2B in complex with AP26113-analog (ALK-IN-1)

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 Residues12
Detailsbinding site for residue E5J A 501
ChainResidue
AGLY172
AALA329
AHOH629
BLEU343
AALA192
APHE267
AGLU268
ALEU269
AVAL270
AASN271
APRO274
ALEU319

site_idAC2
Number of Residues14
Detailsbinding site for residue E5J B 501
ChainResidue
ALEU343
BGLY172
BVAL179
BALA192
BPHE267
BGLU268
BLEU269
BVAL270
BASN271
BLEU319
BALA329
BASP330
BHOH635
BHOH644

site_idAC3
Number of Residues3
Detailsbinding site for residue NA B 502
ChainResidue
BARG290
BASP418
BARG448

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 Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027
ChainResidueDetails
AASP312
BASP312

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
AILE171
ALYS194
BILE171
BLYS194

226707

PDB entries from 2024-10-30

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