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3DVA: 
Snapshots of catalysis in the E1 subunit of the pyruvate dehydrogenase multi-enzyme complex
Biological unit 1: pentameric
Source organism: Geobacillus stearothermophilus
Number of proteins:
5 (Dihydrolipoyllysine-residue acetyltransferase c... ▼)
Protein molecule
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AA -Click to explore this molecule neighborsCC -Click to explore this molecule neighbors
 Pyruvate dehydrogenase E1 component subunit alpha
BB -Click to explore this molecule neighborsDD -Click to explore this molecule neighbors
 Pyruvate dehydrogenase E1 component subunit beta
II -Click to explore this molecule neighbors
 Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
Number of chemicals:
Similar Structures (1607)help
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Showing 1 to 10 out of 1607 selected structures help
      PDB ID Description Taxonomy▲▼ Aligned Protein▲▼ RMSD▲▼ Aligned Residues▲▼ Sequence Identity▲▼
1
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Partial
 3DUF
Snapshots of catalysis in the E1 subunit of the pyruvate dehydrogenase multi-enzyme complex
Others
 4 0.46Å 1378 99%
2
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Partial
 1W85
The crystal structure of pyruvate dehydrogenase E1 bound to the peripheral subunit binding domain of E2
Geobacillus stearothermophilus
 4 0.31Å 1371 99%
3
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Partial
 3DV0
Snapshots of catalysis in the E1 subunit of the pyruvate dehydrogenase multi-enzyme complex
Others
 4 0.27Å 1347 99%
4
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Partial
 1UMD
branched-chain 2-oxo acid dehydrogenase (E1) from Thermus thermophilus HB8 with 4-methyl-2-oxopentanoate as an intermediate
Thermus thermophilus
 4 1.57Å 1337 45%
5
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Partial
 1UMB
branched-chain 2-oxo acid dehydrogenase (E1) from Thermus thermophilus HB8 in holo-form
Thermus thermophilus
 4 1.57Å 1337 45%
6
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Partial
 1UMC
branched-chain 2-oxo acid dehydrogenase (E1) from Thermus thermophilus HB8 with 4-methylpentanoate
Thermus thermophilus
 4 1.62Å 1337 45%
7
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Partial
 1DTW
HUMAN BRANCHED-CHAIN ALPHA-KETO ACID DEHYDROGENASE
Homo sapiens
 4 1.92Å 1336 35%
8
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Partial
 2BFF
Reactivity modulation of human branched-chain alpha-ketoacid dehydrogenase by an internal molecular switch
Homo sapiens
 4 1.82Å 1333 36%
9
Expand row
Partial
 1W88
The crystal structure of pyruvate dehydrogenase E1(D180N,E183Q) bound to the peripheral subunit binding domain of E2
Geobacillus stearothermophilus
 4 0.37Å 1331 99%
10
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Partial
 1U5B
Crystal structure of the human mitochondrial branched-chain alpha-ketoacid dehydrogenase
Homo sapiens
 4 1.79Å 1330 36%
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{"1":"Pyruvate dehydrogenase E1 component subunit alpha","2":"Pyruvate dehydrogenase E1 component subunit beta","3":"Pyruvate dehydrogenase E1 component subunit alpha","4":"Pyruvate dehydrogenase E1 component subunit beta","9":"Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex"}
Citing VAST
Gibrat JF, Madej T, Bryant SH. "Surprising similarities in structure comparison.", Curr Opin Struct Biol.1996 Jun;6(3):377-85
Madej T, Lanczycki CJ, Zhang D, Thiessen PA, Geer RC, Marchler-Bauer A, Bryant SH. "MMDB and VAST+: tracking structural similarities between macromolecular complexes." Nucl. Acids Res. 2014 Jan;42(Database issue):D297-303
Thomas Madej, Aron Marchler-Bauer, Christopher Lanczycki, Dachuan Zhang, Stephen H Bryant "Biological Assembly Comparison With VAST" Methods Mol. Biol. 2020(2112):175-186
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?Original VAST
Original VAST finds structures that are similar to individual protein molecules, or individual 3D domains, in your query structure. Select a protein molecule ("chain") or 3D domain of interest from the table below to view a list of other proteins or domains that have a similar 3D shape. In contrast to VAST+, which focuses on the default biological unit, Original VAST lists all protein molecules in the asymmetric unit of the query structure.