Structure of PDB 3duf Chain G

Receptor sequence
>3dufG (length=365) Species: 1422 (Geobacillus stearothermophilus) [Search protein sequence]
TFQFPFAEQLEKVAEQFPTFQILNEEGEVVNEEAMPELSDEQLKELMRRM
VYTRILDQRSISLNRQGRLGFYAPTAGQEASQIASHFALEKEDFILPGYR
DVPQIIWHGLPLYQAFLFSRGHFHGNQIPEGVNVLPPQIIIGAQYIQAAG
VALGLKMRGKKAVAITYTGDGGTSQGDFYEGINFAGAFKAPAIFVVQNNR
FAISTPVEKQTVAKTLAQKAVAAGIPGIQVDGMDPLAVYAAVKAARERAI
NGEGPTLIETLCFRYGPHTMSGDDPTRYRSKELENEWAKKDPLVRFRKFL
EAKGLWSEEEENNVIEQAKEEIKEAIKKADETPKQKVTDLISIMFEELPF
NLKEQYEIYKEKESK
3D structure
PDB3duf Snapshots of catalysis in the e1 subunit of the pyruvate dehydrogenase multienzyme complex
ChainG
Resolution2.5 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) S65 I142 R267 H271 T272 Y281
Catalytic site (residue number reindexed from 1) S62 I139 R264 H268 T269 Y278
Enzyme Commision number 1.2.4.1: pyruvate dehydrogenase (acetyl-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 G D173 N202 F204 D170 N199 F201
BS02 R1T G Y102 R103 I142 I144 G172 D173 N202 F204 A205 I206 Y99 R100 I139 I141 G169 D170 N199 F201 A202 I203
Gene Ontology
Molecular Function
GO:0004739 pyruvate dehydrogenase (acetyl-transferring) activity
GO:0005515 protein binding
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:3duf, PDBe:3duf, PDBj:3duf
PDBsum3duf
PubMed19081062
UniProtP21873|ODPA_GEOSE Pyruvate dehydrogenase E1 component subunit alpha (Gene Name=pdhA)

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