Structure of PDB 1qs0 Chain A

Receptor sequence
>1qs0A (length=407) Species: 303 (Pseudomonas putida) [Search protein sequence]
NEYAPLRLHVPEPTGRPGCQTDFSYLRLNDAGQARKPPVDVDAADTADLS
YSLVRVLDEQGDAQGPWAEDIDPQILRQGMRAMLKTRIFDSRMVVAQRQK
KMSFYMQSLGEEAIGSGQALALNRTDMCFPTYRQQSILMARDVSLVEMIC
QLLSNERDPLKGRQLPIMYSVREAGFFTISGNLATQFVQAVGWAMASAIK
GDTKIASAWIGDGATAESDFHTALTFAHVYRAPVILNVVNNQWAISTFQA
IAGGESTTFAGRGVGCGIASLRVDGNDFVAVYAASRWAAERARRGLGPSL
IEWVTYRAGPHSTSDDPSKYRPADDWSHFPLGDPIARLKQHLIKIGHWSE
EEHQATTAEFEAAVIAAQKEAEQYGTLANGHIPSAASMFEDVYKEMPDHL
RRQRQEL
3D structure
PDB1qs0 Crystal structure of 2-oxoisovalerate and dehydrogenase and the architecture of 2-oxo acid dehydrogenase multienzyme complexes.
ChainA
Resolution2.4 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) V96 G182 R308 H312 S313 Y321
Catalytic site (residue number reindexed from 1) V95 G181 R307 H311 S312 Y320
Enzyme Commision number 1.2.4.4: 3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring).
Interaction with ligand
Site
#
Ligand Ligand
chain
Binding residues on receptor
(original residue number in PDB)
Binding residues on receptor
(residue number reindexed from 1)
Binding affinity
BS01 MG A D213 N242 W244 D212 N241 W243
BS02 TPP A Y133 R134 L184 G212 D213 G214 A215 N242 W244 A245 I246 H312 Y132 R133 L183 G211 D212 G213 A214 N241 W243 A244 I245 H311
Gene Ontology
Molecular Function
GO:0003863 3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring) activity
GO:0016491 oxidoreductase activity
GO:0016624 oxidoreductase activity, acting on the aldehyde or oxo group of donors, disulfide as acceptor
Biological Process
GO:0009083 branched-chain amino acid catabolic process

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Molecular Function

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Biological Process
External links
PDB RCSB:1qs0, PDBe:1qs0, PDBj:1qs0
PDBsum1qs0
PubMed10426958
UniProtP09060|ODBA_PSEPU 2-oxoisovalerate dehydrogenase subunit alpha (Gene Name=bkdA1)

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