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3CRK

Crystal structure of the PDHK2-L2 complex.

Functional Information from GO Data
ChainGOidnamespacecontents
A0004672molecular_functionprotein kinase activity
A0004674molecular_functionprotein serine/threonine kinase activity
A0004740molecular_functionpyruvate dehydrogenase (acetyl-transferring) kinase activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005739cellular_componentmitochondrion
A0005759cellular_componentmitochondrial matrix
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
A0018105biological_processpeptidyl-serine phosphorylation
A0031670biological_processcellular response to nutrient
A0034614biological_processcellular response to reactive oxygen species
A0042593biological_processglucose homeostasis
A0042802molecular_functionidentical protein binding
A0042803molecular_functionprotein homodimerization activity
A0044877molecular_functionprotein-containing complex binding
A0045254cellular_componentpyruvate dehydrogenase complex
A0050848biological_processregulation of calcium-mediated signaling
A0072332biological_processintrinsic apoptotic signaling pathway by p53 class mediator
B0004672molecular_functionprotein kinase activity
B0004674molecular_functionprotein serine/threonine kinase activity
B0004740molecular_functionpyruvate dehydrogenase (acetyl-transferring) kinase activity
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0005739cellular_componentmitochondrion
B0005759cellular_componentmitochondrial matrix
B0006111biological_processregulation of gluconeogenesis
B0006885biological_processregulation of pH
B0008286biological_processinsulin receptor signaling pathway
B0010510biological_processregulation of acetyl-CoA biosynthetic process from pyruvate
B0010565biological_processregulation of cellular ketone metabolic process
B0010906biological_processregulation of glucose metabolic process
B0016301molecular_functionkinase activity
B0018105biological_processpeptidyl-serine phosphorylation
B0031670biological_processcellular response to nutrient
B0034614biological_processcellular response to reactive oxygen species
B0042593biological_processglucose homeostasis
B0042802molecular_functionidentical protein binding
B0042803molecular_functionprotein homodimerization activity
B0044877molecular_functionprotein-containing complex binding
B0045254cellular_componentpyruvate dehydrogenase complex
B0050848biological_processregulation of calcium-mediated signaling
B0072332biological_processintrinsic apoptotic signaling pathway by p53 class mediator
C0006086biological_processacetyl-CoA biosynthetic process from pyruvate
C0045254cellular_componentpyruvate dehydrogenase complex
D0006086biological_processacetyl-CoA biosynthetic process from pyruvate
D0045254cellular_componentpyruvate dehydrogenase complex
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE K A 3001
ChainResidue
ASER24
APHE26
AASN63
ATYR374

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE K B 3002
ChainResidue
BSER24
BPHE26
BASN63
BTYR374

Functional Information from PROSITE/UniProt
site_idPS00178
Number of Residues12
DetailsAA_TRNA_LIGASE_I Aminoacyl-transfer RNA synthetases class-I signature. PalSPtMTMGTV
ChainResidueDetails
CPRO138-VAL149

site_idPS00189
Number of Residues30
DetailsLIPOYL 2-oxo acid dehydrogenases acyltransferase component lipoyl binding site. GekLsegDLLaeIETdKATigFevqeeGyL
ChainResidueDetails
CGLY157-LEU186

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsBINDING:
ChainResidueDetails
AGLU251
AASP290
ASER309
AGLY325
BGLU251
BASP290
BSER309
BGLY325

site_idSWS_FT_FI2
Number of Residues4
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:Q15118
ChainResidueDetails
ATYR215
ATYR216
BTYR215
BTYR216

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:Q8BFP9
ChainResidueDetails
ALYS376
BLYS376

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1jm6
ChainResidueDetails
AGLU251
AHIS247

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1jm6
ChainResidueDetails
BGLU251
BHIS247

site_idMCSA1
Number of Residues4
DetailsM-CSA 603
ChainResidueDetails
AHIS247electrostatic stabiliser
AGLU251metal ligand, proton shuttle (general acid/base)
ALYS254metal ligand
AASN255metal ligand

site_idMCSA2
Number of Residues4
DetailsM-CSA 603
ChainResidueDetails
BHIS247electrostatic stabiliser
BGLU251metal ligand, proton shuttle (general acid/base)
BLYS254metal ligand
BASN255metal ligand

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PDB entries from 2024-05-01

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