Structure of PDB 3duf Chain E

Receptor sequence

>3dufE (length=365) Species: 1422 (Geobacillus stearothermophilus)

TFQFPFAEQLEKVAEQFPTFQILNEEGEVVNEEAMPELSDEQLKELMRRM
VYTRILDQRSISLNRQGRLGFYAPTAGQEASQIASHFALEKEDFILPGYR
DVPQIIWHGLPLYQAFLFSRGHFHGNQIPEGVNVLPPQIIIGAQYIQAAG
VALGLKMRGKKAVAITYTGDGGTSQGDFYEGINFAGAFKAPAIFVVQNNR
FAISTPVEKQTVAKTLAQKAVAAGIPGIQVDGMDPLAVYAAVKAARERAI
NGEGPTLIETLCFRYGPHTMSGDDPTRYRSKELENEWAKKDPLVRFRKFL
EAKGLWSEEEENNVIEQAKEEIKEAIKKADETPKQKVTDLISIMFEELPF
NLKEQYEIYKEKESK

3D structure

• PDB: 3duf Snapshots of catalysis in the e1 subunit of the pyruvate dehydrogenase multienzyme complex
• Chain: E
• Resolution: 2.5 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): S65 I143
• Catalytic site (residue number reindexed from 1): S62 I140
• 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	E	D173 N202 F204	D170 N199 F201
BS02	R1T	E	Y102 R103 I142 I144 G172 D173 G174 F204 I206 H271	Y99 R100 I139 I141 G169 D170 G171 F201 I203 H268

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

External links

• PDB: RCSB:3duf, PDBe:3duf, PDBj:3duf
• PDBsum: 3duf
• PubMed: 19081062
• UniProt: P21873|ODPA_GEOSE Pyruvate dehydrogenase E1 component subunit alpha (Gene Name=pdhA)