3TZ2

Crystal structure of branched-chain alpha-ketoacid dehydrogenase kinase/phenylbutyrate 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	0004722	molecular_function	protein serine/threonine phosphatase activity
A	0004740	molecular_function	pyruvate dehydrogenase (acetyl-transferring) kinase activity
A	0005524	molecular_function	ATP binding
A	0005739	cellular_component	mitochondrion
A	0005759	cellular_component	mitochondrial matrix
A	0006550	biological_process	isoleucine catabolic process
A	0006552	biological_process	L-leucine catabolic process
A	0006574	biological_process	valine catabolic process
A	0007283	biological_process	spermatogenesis
A	0008610	biological_process	lipid biosynthetic process
A	0009083	biological_process	branched-chain amino acid catabolic process
A	0009353	cellular_component	obsolete mitochondrial oxoglutarate dehydrogenase complex
A	0010906	biological_process	regulation of glucose metabolic process
A	0016301	molecular_function	kinase activity
A	0016310	biological_process	phosphorylation
A	0016740	molecular_function	transferase activity
A	0016772	molecular_function	transferase activity, transferring phosphorus-containing groups
A	0047323	molecular_function	[3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring)] kinase activity
A	0106310	molecular_function	protein serine kinase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	8
Details	BINDING SITE FOR RESIDUE CLT A 389

Chain	Residue
A	LEU68
A	TYR99
A	LEU128
A	LEU129
A	HIS132
A	ARG167
A	ILE170
A	ARG171

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	10
Details	BINDING: BINDING => ECO:0000269|PubMed:11562470, ECO:0007744|PDB:1GKZ

Chain	Residue	Details
A	ASN249
A	LEU340
A	ASP285
A	VAL298
A	ASP300
A	PHE303
A	THR304
A	THR305
A	HIS334
A	GLY337

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site_id	SWS_FT_FI2
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0000269|PubMed:7649998, ECO:0007744|PubMed:22673903

Chain	Residue	Details
A	SER1

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site_id	SWS_FT_FI3
Number of Residues	2
Details	MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:O14874

Chain	Residue	Details
A	LYS162
A	LYS203

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site_id	SWS_FT_FI4
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:22673903

Chain	Residue	Details
A	SER326
A	SER330

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