Assemblies
Multimeric state:
hetero octamer
Accessible surface area:
78318.62 Å2
Buried surface area:
15929.8 Å2
Dissociation area:
677.39
Å2
Dissociation energy (ΔGdiss):
4.06
kcal/mol
Dissociation entropy (TΔSdiss):
12.28
kcal/mol
Symmetry number:
4
PDBe Complex ID:
PDB-CPX-142043
Macromolecules
Chains: A, C, E, F
Length: 449 amino acids
Theoretical weight: 49.39 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli BL21(DE3)
UniProt:
Pfam:
Length: 449 amino acids
Theoretical weight: 49.39 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical:
P24182 (Residues: 1-449; Coverage: 100%)
Pfam:
- Biotin carboxylase, N-terminal domain
- Carbamoyl-phosphate synthase L chain, ATP binding domain
- Biotin carboxylase C-terminal domain
- Acetyl-CoA carboxylase, biotin carboxylase
- Biotin carboxylase-like, N-terminal domain
- Biotin carboxylation domain
- Pre-ATP-grasp domain superfamily
- Carbamoyl-phosphate synthetase large subunit-like, ATP-binding domain
- ATP-grasp fold
- ATP-grasp fold, subdomain 1
- Rudiment single hybrid motif
- Biotin carboxylase, C-terminal
Chains: B, D, G, I
Length: 176 amino acids
Theoretical weight: 18.87 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli BL21(DE3)
UniProt:
Pfam: Biotin-requiring enzyme
InterPro:
CATH: OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Length: 176 amino acids
Theoretical weight: 18.87 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical: P0ABD8 (Residues: 1-156; Coverage: 100%)
Pfam: Biotin-requiring enzyme
InterPro:
CATH: OB fold (Dihydrolipoamide Acetyltransferase, E2P)
