Assemblies
Assembly Name:
Pyruvate dehydrogenase E1 heterotetramer
Multimeric state:
hetero tetramer
Accessible surface area:
42348.25 Å2
Buried surface area:
22244.77 Å2
Dissociation area:
6,294.77
Å2
Dissociation energy (ΔGdiss):
102.3
kcal/mol
Dissociation entropy (TΔSdiss):
16.76
kcal/mol
Symmetry number:
2
PDBe Complex ID:
PDB-CPX-140174
Macromolecules
Chains: A, C
Length: 365 amino acids
Theoretical weight: 41.28 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Pfam: Dehydrogenase E1 component
InterPro:
SCOP: Branched-chain alpha-keto acid dehydrogenase PP module
Length: 365 amino acids
Theoretical weight: 41.28 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical:
P08559 (Residues: 30-390; Coverage: 93%)
Pfam: Dehydrogenase E1 component
InterPro:
- Thiamin diphosphate-binding fold
- Pyruvate dehydrogenase (acetyl-transferring) E1 component, alpha subunit, subgroup y
- Dehydrogenase, E1 component
SCOP: Branched-chain alpha-keto acid dehydrogenase PP module
Chains: B, D
Length: 341 amino acids
Theoretical weight: 37.96 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Pfam:
InterPro:
SCOP:
Length: 341 amino acids
Theoretical weight: 37.96 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical:
P11177 (Residues: 31-359; Coverage: 92%)
Pfam:
InterPro:
- Thiamin diphosphate-binding fold
- Pyruvate dehydrogenase E1 component subunit beta
- Transketolase-like, pyrimidine-binding domain
- Transketolase C-terminal/Pyruvate-ferredoxin oxidoreductase domain II
- Transketolase, C-terminal domain
SCOP: