Structure of PDB 1w85 Chain A

Receptor sequence
>1w85A (length=358) Species: 1422 (Geobacillus stearothermophilus) [Search protein sequence]
TFQFPFAEQLEKVAEQFPTFQILNEEGEVVNEEAMPELSDEQLKELMRRM
VYTRILDQRSISLNRQGRLGFYAPTAGQEASQIASHFALEKEDFILPGYR
DVPQIIWHGLPLYQAFLFSRGHFHGNQIPEGVNVLPPQIIIGAQYIQAAG
VALGLKMRGKKAVAITYTGDGGTSQGDFYEGINFAGAFKAPAIFVVQNNR
FAISTPVEKQTVAKTLAQKAVAAGIPGIQVDGMDPLAVYAAVKAARERAI
NGEGPTLIETLCFRYGPHTMSGDSKELENEWAKKDPLVRFRKFLEAKGLW
SEEEENNVIEQAKEEIKEAIKKADETPKQKVTDLISIMFEELPFNLKEQY
EIYKEKES
3D structure
PDB1w85 A molecular switch and proton wire synchronize the active sites in thiamine enzymes.
ChainA
Resolution2.0 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
Catalytic site (residue number reindexed from 1) S62 I139 R264 H268 T269
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 A D173 N202 F204 D170 N199 F201
BS02 TPP A Y102 R103 I142 I144 G172 D173 G174 G175 N202 A205 I206 H271 Y99 R100 I139 I141 G169 D170 G171 G172 N199 A202 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

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Molecular Function
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Biological Process
External links
PDB RCSB:1w85, PDBe:1w85, PDBj:1w85
PDBsum1w85
PubMed15514159
UniProtP21873|ODPA_GEOSE Pyruvate dehydrogenase E1 component subunit alpha (Gene Name=pdhA)

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