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6BQP

Crystal Structure of the Human CAMKK2B in complex with Crenolanib

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 6T2 A 501
ChainResidue
AILE171
AGLY273
ASER316
AASN317
ALEU319
AASP330
AHOH644
AHOH659
AVAL179
AALA192
APHE267
AGLU268
ALEU269
AVAL270
AASN271
AGLN272

site_idAC2
Number of Residues4
Detailsbinding site for residue EDO A 502
ChainResidue
ATYR190
ATYR191
AGLU268
ALEU269

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
ALYS194
AILE171

219140

PDB entries from 2024-05-01

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