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5YVC

Structure of CaMKK2 in complex with CKI-012

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 Residues12
Detailsbinding site for residue SU6 A 501
ChainResidue
AILE171
ALEU319
AASP330
AGOL504
AALA192
ALYS194
APHE267
AGLU268
ALEU269
AVAL270
AASN271
AGLY273

site_idAC2
Number of Residues6
Detailsbinding site for residue GOL A 502
ChainResidue
AARG394
AGLU432
ASER433
AARG434
AGLU439
AHOH722

site_idAC3
Number of Residues1
Detailsbinding site for residue GOL A 503
ChainResidue
AGLN288

site_idAC4
Number of Residues7
Detailsbinding site for residue GOL A 504
ChainResidue
AASN271
APHE337
ALYS338
AASP341
ALEU343
ASU6501
AHOH616

site_idAC5
Number of Residues6
Detailsbinding site for residue PGE A 505
ChainResidue
AARG394
AARG425
AHOH601
AHOH602
AHOH672
AHOH693

site_idAC6
Number of Residues3
Detailsbinding site for residue CL A 506
ChainResidue
APRO315
ASER316
AHOH787

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

223532

PDB entries from 2024-08-07

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