Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2PNR

Crystal Structure of the asymmetric Pdk3-l2 Complex

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0004672	molecular_function	protein kinase activity
A	0004674	molecular_function	protein serine/threonine kinase activity
A	0004740	molecular_function	pyruvate dehydrogenase (acetyl-transferring) kinase activity
A	0005515	molecular_function	protein binding
A	0005524	molecular_function	ATP binding
A	0005730	cellular_component	nucleolus
A	0005739	cellular_component	mitochondrion
A	0005759	cellular_component	mitochondrial matrix
A	0010510	biological_process	regulation of pyruvate decarboxylation to acetyl-CoA
A	0010906	biological_process	regulation of glucose metabolic process
A	0016301	molecular_function	kinase activity
A	0016740	molecular_function	transferase activity
A	0018105	biological_process	peptidyl-serine phosphorylation
A	0033554	biological_process	cellular response to stress
A	0035357	biological_process	peroxisome proliferator activated receptor signaling pathway
A	0071333	biological_process	cellular response to glucose stimulus
A	0071398	biological_process	cellular response to fatty acid
A	0097411	biological_process	hypoxia-inducible factor-1alpha signaling pathway
A	2000377	biological_process	regulation of reactive oxygen species metabolic process
B	0000166	molecular_function	nucleotide binding
B	0004672	molecular_function	protein kinase activity
B	0004674	molecular_function	protein serine/threonine kinase activity
B	0004740	molecular_function	pyruvate dehydrogenase (acetyl-transferring) kinase activity
B	0005515	molecular_function	protein binding
B	0005524	molecular_function	ATP binding
B	0005730	cellular_component	nucleolus
B	0005739	cellular_component	mitochondrion
B	0005759	cellular_component	mitochondrial matrix
B	0010510	biological_process	regulation of pyruvate decarboxylation to acetyl-CoA
B	0010906	biological_process	regulation of glucose metabolic process
B	0016301	molecular_function	kinase activity
B	0016740	molecular_function	transferase activity
B	0018105	biological_process	peptidyl-serine phosphorylation
B	0033554	biological_process	cellular response to stress
B	0035357	biological_process	peroxisome proliferator activated receptor signaling pathway
B	0071333	biological_process	cellular response to glucose stimulus
B	0071398	biological_process	cellular response to fatty acid
B	0097411	biological_process	hypoxia-inducible factor-1alpha signaling pathway
B	2000377	biological_process	regulation of reactive oxygen species metabolic process
C	0006086	biological_process	pyruvate decarboxylation to acetyl-CoA
C	0045254	cellular_component	pyruvate dehydrogenase complex
E	0000166	molecular_function	nucleotide binding
E	0004672	molecular_function	protein kinase activity
E	0004674	molecular_function	protein serine/threonine kinase activity
E	0004740	molecular_function	pyruvate dehydrogenase (acetyl-transferring) kinase activity
E	0005515	molecular_function	protein binding
E	0005524	molecular_function	ATP binding
E	0005730	cellular_component	nucleolus
E	0005739	cellular_component	mitochondrion
E	0005759	cellular_component	mitochondrial matrix
E	0010510	biological_process	regulation of pyruvate decarboxylation to acetyl-CoA
E	0010906	biological_process	regulation of glucose metabolic process
E	0016301	molecular_function	kinase activity
E	0016740	molecular_function	transferase activity
E	0018105	biological_process	peptidyl-serine phosphorylation
E	0033554	biological_process	cellular response to stress
E	0035357	biological_process	peroxisome proliferator activated receptor signaling pathway
E	0071333	biological_process	cellular response to glucose stimulus
E	0071398	biological_process	cellular response to fatty acid
E	0097411	biological_process	hypoxia-inducible factor-1alpha signaling pathway
E	2000377	biological_process	regulation of reactive oxygen species metabolic process
F	0000166	molecular_function	nucleotide binding
F	0004672	molecular_function	protein kinase activity
F	0004674	molecular_function	protein serine/threonine kinase activity
F	0004740	molecular_function	pyruvate dehydrogenase (acetyl-transferring) kinase activity
F	0005515	molecular_function	protein binding
F	0005524	molecular_function	ATP binding
F	0005730	cellular_component	nucleolus
F	0005739	cellular_component	mitochondrion
F	0005759	cellular_component	mitochondrial matrix
F	0010510	biological_process	regulation of pyruvate decarboxylation to acetyl-CoA
F	0010906	biological_process	regulation of glucose metabolic process
F	0016301	molecular_function	kinase activity
F	0016740	molecular_function	transferase activity
F	0018105	biological_process	peptidyl-serine phosphorylation
F	0033554	biological_process	cellular response to stress
F	0035357	biological_process	peroxisome proliferator activated receptor signaling pathway
F	0071333	biological_process	cellular response to glucose stimulus
F	0071398	biological_process	cellular response to fatty acid
F	0097411	biological_process	hypoxia-inducible factor-1alpha signaling pathway
F	2000377	biological_process	regulation of reactive oxygen species metabolic process
G	0006086	biological_process	pyruvate decarboxylation to acetyl-CoA
G	0045254	cellular_component	pyruvate dehydrogenase complex

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE RED C 900

Chain	Residue
A	ARG397
B	GLN31
B	PHE35
B	PHE48
C	LYS173
C	HOH906

site_id	AC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE RED G 901

Chain	Residue
E	ARG397
F	LEU27
G	LYS173

Functional Information from PROSITE/UniProt

site_id	PS00178
Number of Residues	12
Details	AA_TRNA_LIGASE_I Aminoacyl-transfer RNA synthetases class-I signature. PalSPtMTMGTV

Chain	Residue	Details
C	PRO138-VAL149

site_id	PS00189
Number of Residues	30
Details	LIPOYL 2-oxo acid dehydrogenases acyltransferase component lipoyl binding site. GekLsegDLLaeIETdKATigFevqeeGyL

Chain	Residue	Details
C	GLY157-LEU186

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	42
Details	Binding site: {"evidences":[{"source":"PubMed","id":"15861126","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	4
Details	Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"Q922H2","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	2
Details	Modified residue: {"description":"N6-lipoyllysine","evidences":[{"source":"PROSITE-ProRule","id":"PRU01066","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"15861126","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17532006","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17683942","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25525879","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1Y8N","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1Y8O","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1Y8P","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2PNR","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2Q8I","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	Annotated By Reference To The Literature 1jm6

Chain	Residue	Details
A	HIS243
A	GLU247

site_id	CSA2
Number of Residues	2
Details	Annotated By Reference To The Literature 1jm6

Chain	Residue	Details
B	HIS243
B	GLU247

site_id	CSA3
Number of Residues	2
Details	Annotated By Reference To The Literature 1jm6

Chain	Residue	Details
E	HIS243
E	GLU247

site_id	CSA4
Number of Residues	2
Details	Annotated By Reference To The Literature 1jm6

Chain	Residue	Details
F	HIS243
F	GLU247

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)