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4MPN

Crystal structure of pyruvate dehydrogenase kinase isoform 2 in complex with inhibitor PS10

Functional Information from GO Data
ChainGOidnamespacecontents
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 acetyl-CoA biosynthetic process from pyruvate
A0010565biological_processregulation of cellular ketone metabolic process
A0010906biological_processregulation of glucose metabolic process
A0016301molecular_functionkinase activity
A0031670biological_processcellular response to nutrient
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 Residues14
DetailsBINDING SITE FOR RESIDUE PV0 A 501
ChainResidue
ALEU252
AHOH602
AHOH609
AHOH688
AHOH720
AHOH735
AASN255
AARG258
AALA259
AGLU262
AASP290
AGLY294
AVAL295
ATHR354

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE TLA A 502
ChainResidue
AGLU262
ASER263
AHIS264
AGLU265
ASER266
AHOH761
AHOH778

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:16401071
ChainResidueDetails
AGLU251
AASP290
AGLY325

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
ASER309

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:Q15118
ChainResidueDetails
ATYR215
ATYR216

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:Q8BFP9
ChainResidueDetails
ALYS376

227111

PDB entries from 2024-11-06

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