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1Y8P

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 Residues3
DetailsBINDING SITE FOR RESIDUE MG A 501
ChainResidue
AASN251
AATP504
AHOH535

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE K A 502
ChainResidue
ASER20
AARG21
APHE22
AASN59
APHE372

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE K A 503
ChainResidue
AASN302
ATYR305
AGLY325
AATP504
ALEU300

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE RED B 373
ChainResidue
ASER45
APHE48
BLYS173

site_idAC5
Number of Residues25
DetailsBINDING SITE FOR RESIDUE ATP A 504
ChainResidue
AGLU247
ALYS250
AASN251
AARG254
AALA255
AASP287
AVAL292
ALEU300
ATYR305
ASER306
ATHR307
ALEU321
AALA322
AGLY323
APHE324
AGLY325
ATYR326
AGLY327
ALEU328
ATHR352
AMG501
AK503
AHOH513
AHOH534
AHOH535

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
AASP287
ASER306
AGLY323

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

218853

PDB entries from 2024-04-24

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