1Y8P

Crystal structure of the PDK3-L2 complex

Functional Information from GO Data

Chain	GOid	namespace	contents
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	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	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	0006086	biological_process	pyruvate decarboxylation to acetyl-CoA
B	0045254	cellular_component	pyruvate dehydrogenase complex

Functional Information from PDB Data

site_id	AC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MG A 501

Chain	Residue
A	ASN251
A	ATP504
A	HOH535

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site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE K A 502

Chain	Residue
A	SER20
A	ARG21
A	PHE22
A	ASN59
A	PHE372

---

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE K A 503

Chain	Residue
A	ASN302
A	TYR305
A	GLY325
A	ATP504
A	LEU300

---

site_id	AC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE RED B 373

Chain	Residue
A	SER45
A	PHE48
B	LYS173

---

site_id	AC5
Number of Residues	25
Details	BINDING SITE FOR RESIDUE ATP A 504

Chain	Residue
A	GLU247
A	LYS250
A	ASN251
A	ARG254
A	ALA255
A	ASP287
A	VAL292
A	LEU300
A	TYR305
A	SER306
A	THR307
A	LEU321
A	ALA322
A	GLY323
A	PHE324
A	GLY325
A	TYR326
A	GLY327
A	LEU328
A	THR352
A	MG501
A	K503
A	HOH513
A	HOH534
A	HOH535

---

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
B	PRO138-VAL149

---

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

Chain	Residue	Details
B	GLY157-LEU186

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	14
Details	Binding site: {"evidences":[{"source":"PubMed","id":"15861126","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	1
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	76
Details	Domain: {"description":"Lipoyl-binding 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU01066","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	1
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

---