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1Y8N

Crystal structure of the PDK3-L2 complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0004672molecular_functionprotein kinase activity
A0004674molecular_functionprotein serine/threonine kinase activity
A0004740molecular_functionpyruvate dehydrogenase (acetyl-transferring) kinase activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005730cellular_componentnucleolus
A0005739cellular_componentmitochondrion
A0005759cellular_componentmitochondrial matrix
A0010510biological_processregulation of acetyl-CoA biosynthetic process from pyruvate
A0010906biological_processregulation of glucose metabolic process
A0016301molecular_functionkinase activity
A0016310biological_processphosphorylation
A0016740molecular_functiontransferase activity
A0018105biological_processpeptidyl-serine phosphorylation
A0035357biological_processperoxisome proliferator activated receptor signaling pathway
A0071333biological_processcellular response to glucose stimulus
A0071398biological_processcellular response to fatty acid
A0097411biological_processhypoxia-inducible factor-1alpha signaling pathway
A2000377biological_processregulation of reactive oxygen species metabolic process
B0006086biological_processacetyl-CoA biosynthetic process from pyruvate
B0045254cellular_componentpyruvate dehydrogenase complex
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE K A 501
ChainResidue
ASER20
AARG21
APHE22
AASN59
APHE372

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE RED B 373
ChainResidue
APHE48
BLYS173

Functional Information from PROSITE/UniProt
site_idPS00178
Number of Residues12
DetailsAA_TRNA_LIGASE_I Aminoacyl-transfer RNA synthetases class-I signature. PalSPtMTMGTV
ChainResidueDetails
BPRO138-VAL149

site_idPS00189
Number of Residues30
DetailsLIPOYL 2-oxo acid dehydrogenases acyltransferase component lipoyl binding site. GekLsegDLLaeIETdKATigFevqeeGyL
ChainResidueDetails
BGLY157-LEU186

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsMOD_RES: N6-lipoyllysine => ECO:0000255|PROSITE-ProRule:PRU01066, ECO:0000269|PubMed:15861126, ECO:0000269|PubMed:17532006, ECO:0000269|PubMed:17683942, ECO:0000269|PubMed:25525879, ECO:0007744|PDB:1Y8N, ECO:0007744|PDB:1Y8O, ECO:0007744|PDB:1Y8P, ECO:0007744|PDB:2PNR, ECO:0007744|PDB:2Q8I
ChainResidueDetails
BILE206
AGLY323
AASP287
ASER306

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:Q922H2
ChainResidueDetails
ALYS278

218500

PDB entries from 2024-04-17

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