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2BU5

crystal structures of human pyruvate dehydrogenase kinase 2 containing physiological and synthetic ligands

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0004672molecular_functionprotein kinase activity
A0004740molecular_functionpyruvate dehydrogenase (acetyl-transferring) kinase activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005654cellular_componentnucleoplasm
A0005739cellular_componentmitochondrion
A0005759cellular_componentmitochondrial matrix
A0005829cellular_componentcytosol
A0006006biological_processglucose metabolic process
A0006111biological_processregulation of gluconeogenesis
A0006885biological_processregulation of pH
A0008286biological_processinsulin receptor signaling pathway
A0010510biological_processregulation of pyruvate decarboxylation to acetyl-CoA
A0010565biological_processregulation of ketone metabolic process
A0010906biological_processregulation of glucose metabolic process
A0016301molecular_functionkinase activity
A0016740molecular_functiontransferase activity
A0031670biological_processcellular response to nutrient
A0033554biological_processcellular response to stress
A0034614biological_processcellular response to reactive oxygen species
A0042593biological_processglucose homeostasis
A0042803molecular_functionprotein homodimerization activity
A0045254cellular_componentpyruvate dehydrogenase complex
A0050848biological_processregulation of calcium-mediated signaling
A0072332biological_processintrinsic apoptotic signaling pathway by p53 class mediator
Functional Information from PDB Data
site_idAC1
Number of Residues9
DetailsBINDING SITE FOR RESIDUE TF1 A1386
ChainResidue
ALEU23
AGLN27
APHE28
APHE31
ASER41
APHE44
ALEU45
ALEU160
AGLN163

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"16401071","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"Q15118","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsModified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"Q8BFP9","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1jm6
ChainResidueDetails
AGLU243
AHIS239

238582

PDB entries from 2025-07-09

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