Structure analysis

CRYSTAL STRUCTURE OF THE SECA PROTEIN TRANSLOCATION ATPASE FROM MYCOBACTERIUM TUBERCULOSIS in APO FORM

X-ray diffraction
2.8Å resolution
Source organism: Mycobacterium tuberculosis
Assemblies composition:
homo dimer (preferred)
homo tetramer
Entry contents: 1 distinct polypeptide molecule

Assemblies

Assembly 1 (preferred)
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Multimeric state: homo dimer
Accessible surface area: 74700 Å2
Buried surface area: 2700 Å2
Dissociation area: 1,300 Å2
Dissociation energy (ΔGdiss): 9 kcal/mol
Dissociation entropy (TΔSdiss): 16 kcal/mol
Interface energy (ΔGint): -21 kcal/mol
Symmetry number: 2
Assembly 2
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Multimeric state: homo tetramer
Accessible surface area: 141200 Å2
Buried surface area: 13500 Å2
Dissociation area: 2,700 Å2
Dissociation energy (ΔGdiss): 32 kcal/mol
Dissociation entropy (TΔSdiss): 18 kcal/mol
Interface energy (ΔGint): -89 kcal/mol
Symmetry number: 4

Macromolecules

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