Structure analysis

Structure of the acetoacetyl-CoA-thiolase/HMG-CoA-synthase complex from Methanothermococcus thermolithotrophicus at 2.75 A

X-ray diffraction
2.75Å resolution
Assembly composition:
hetero dodecamer (preferred)
Entry contents: 3 distinct polypeptide molecules

Assemblies

Assembly 1 (preferred)
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Multimeric state: hetero dodecamer
Accessible surface area: 101543.99 Å2
Buried surface area: 57590.1 Å2
Dissociation area: 461.25 Å2
Dissociation energy (ΔGdiss): -4.24 kcal/mol
Dissociation entropy (TΔSdiss): 0.21 kcal/mol
Symmetry number: 4
PDBe Complex ID: PDB-CPX-104734

Macromolecules

Chains: A, B, C, D
Length: 392 amino acids
Theoretical weight: 41.94 KDa
Source organism: Methanothermococcus thermolithotrophicus
UniProt:
  • Canonical: A0A384E138 (Residues: 1-392; Coverage: 100%)
Pfam:
InterPro:
PDBe-KB: UniProt Coverage View: A0A384E138  
139250100150200250300350
 
100200300
UniProt
A0A384E138
Chains
Domains
Secondary structure
Flexibility predictions
Early folding residue predictions
Ligand binding sites
Interaction interfaces
Sequence conservation

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Chains: E, F, G, H
Length: 130 amino acids
Theoretical weight: 14.91 KDa
Source organism: Methanothermococcus thermolithotrophicus
UniProt:
  • Canonical: A0A384E139 (Residues: 1-130; Coverage: 100%)
Pfam:
InterPro:
PDBe-KB: UniProt Coverage View: A0A384E139  
1130102030405060708090100110120130
 
50100MVVRSWRHMKERYNLIGTRCKTCGKVYFPSRTVCPDCRRKGELEEFQLSGKGKIYTYSIVYAPPKEFNKLTPYVIAIVELEEGPKVTAQVDCDINKISIGIPVEAAFRRIKEDGKDGIISYGYKFVPITE
UniProt
A0A384E139
Chains
Domains
Secondary structure
Flexibility predictions
Early folding residue predictions
Ligand binding sites
Interaction interfaces
Sequence conservation

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PDBe-KB: UniProt Coverage View: A0A384E143  
134950100150200250300
 
100200300
UniProt
A0A384E143
Chains
Domains
Secondary structure
Flexibility predictions
Early folding residue predictions
Ligand binding sites
Interaction interfaces
Sequence conservation

Search similar proteins