Structure of PDB 1w88 Chain E

Receptor sequence
>1w88E (length=328) Species: 1422 (Geobacillus stearothermophilus) [Search protein sequence]
FQFPFAEQLEKVAEQFPTFQILNEEGEVVNEEAMPELSDEQLKELMRRMV
YTRILDQRSISLNRQGRLGFYAPTAGQEASQIASHFALEKEDFILPGYRD
VPQIIWHGLPLYQAFLFSRGHFHGNQIPEGVNVLPPQIIIGAQYIQAAGV
ALGLKMRGKKAVAITYTGDGGTSQGNFYQGINFAGAFKAPAIFVVQNNRF
AAKTLAQKAVAAGIPGIQVDGMDPLAVYAAVKAARERAINGEGPTLIETL
CKKDPLVRFRKFLEAKGLWSEEEENNVIEQAKEEIKEAIKKADETPKQKV
TDLISIMFEELPFNLKEQYEIYKEKESK
3D structure
PDB1w88 A Molecular Switch and Proton-Wire Synchronize the Active Sites in Thiamine-Dependent Enzymes
ChainE
Resolution2.3 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
Catalytic site (residue number reindexed from 1) S61 I138
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 D169 N198
BS02 TPP E Y102 R103 I144 D173 G174 Y98 R99 I140 D169 G170
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:1w88, PDBe:1w88, PDBj:1w88
PDBsum1w88
PubMed15514159
UniProtP21873|ODPA_GEOSE Pyruvate dehydrogenase E1 component subunit alpha (Gene Name=pdhA)

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