Structure analysis

The structural versatility of TasA in B. subtilis biofilm formation

X-ray diffraction
1.56Å resolution
Assembly composition:
monomeric (preferred)
Entry contents: 1 distinct polypeptide molecule

Assemblies

Assembly 1 (preferred)
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Multimeric state: monomeric
Accessible surface area: 10947.17 Ã…2
Buried surface area: 1004.17 Ã…2
Dissociation area: 199.45 Ã…2
Dissociation energy (ΔGdiss): -4.44 kcal/mol
Dissociation entropy (TΔSdiss): 1.98 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-157033
Assembly 2
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Multimeric state: monomeric
Accessible surface area: 10570.12 Ã…2
Buried surface area: 359.65 Ã…2
Dissociation area: 179.83 Ã…2
Dissociation energy (ΔGdiss): -5.6 kcal/mol
Dissociation entropy (TΔSdiss): 1.97 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-157033

Macromolecules

Chains: A, B
Length: 210 amino acids
Theoretical weight: 23.16 KDa
Source organism: Bacillus subtilis subsp. subtilis str. 168
Expression system: Escherichia coli
UniProt:
  • Canonical: P54507 (Residues: 30-239; Coverage: 90%)
Gene names: BSU24620, cotN, tasA, yqhF
Pfam: Camelysin metallo-endopeptidase
InterPro: Peptidase M73, camelysin

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