Structure of PDB 1w85 Chain G

Receptor sequence
>1w85G (length=364) Species: 1422 (Geobacillus stearothermophilus) [Search protein sequence]
FQFPFAEQLEKVAEQFPTFQILNEEGEVVNEEAMPELSDEQLKELMRRMV
YTRILDQRSISLNRQGRLGFYAPTAGQEASQIASHFALEKEDFILPGYRD
VPQIIWHGLPLYQAFLFSRGHFHGNQIPEGVNVLPPQIIIGAQYIQAAGV
ALGLKMRGKKAVAITYTGDGGTSQGDFYEGINFAGAFKAPAIFVVQNNRF
AISTPVEKQTVAKTLAQKAVAAGIPGIQVDGMDPLAVYAAVKAARERAIN
GEGPTLIETLCFRYGPHTMSGDDPTRYRSKELENEWAKKDPLVRFRKFLE
AKGLWSEEEENNVIEQAKEEIKEAIKKADETPKQKVTDLISIMFEELPFN
LKEQYEIYKEKESK
3D structure
PDB1w85 A molecular switch and proton wire synchronize the active sites in thiamine enzymes.
ChainG
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 Y281
Catalytic site (residue number reindexed from 1) S61 I138 R263 H267 T268 Y277
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 D169 N198 F200
BS02 TPP G Y102 R103 I142 I144 G172 D173 G174 G175 N202 A205 I206 H271 Y98 R99 I138 I140 G168 D169 G170 G171 N198 A201 I202 H267
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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