Structure of PDB 3dv0 Chain E

Receptor sequence

>3dv0E (length=344) Species: 1422 (Geobacillus stearothermophilus)

TFQFPFAEQLEKVAEQFPTFQILNEEGEVVNEEAMPELSDEQLKELMRRM
VYTRILDQRSISLNRQGRLGFYAPTAGQEASQIASHFALEKEDFILPGYR
DVPQIIWHGLPLYQAFLFSRGHFHGNQIPEGVNVLPPQIIIGAQYIQAAG
VALGLKMRGKKAVAITYTGDGGTSQGDFYEGINFAGAFKAPAIFVVQNNR
FAISTPVEKQTVAKTLAQKAVAAGIPGIQVDGMDPLAVYAAVKAARERAI
NGEGPTLIETLCFRYEWAKKDPLVRFRKFLEAKGLWSEEEENNVIEQAKE
EIKEAIKKADETPKQKVTDLISIMFEELPFNLKEQYEIYKEKES

3D structure

• PDB: 3dv0 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 I142 R267
• Catalytic site (residue number reindexed from 1): S62 I139 R264
• 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	TPW	E	Y102 R103 I142 I144 G172 D173 G174 N202 F204 A205 I206	Y99 R100 I139 I141 G169 D170 G171 N199 F201 A202 I203
BS02	MG	E	G172 D173 Q200 N202	G169 D170 Q197 N199

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:3dv0, PDBe:3dv0, PDBj:3dv0
• PDBsum: 3dv0
• PubMed: 19081062
• UniProt: P21873|ODPA_GEOSE Pyruvate dehydrogenase E1 component subunit alpha (Gene Name=pdhA)