Structure analysis

Structure of the D-Erythrose-4-Phosphate Dehydrogenase from E. coli in complex with a NAD cofactor analog (3-Chloroacetyl adenine pyridine dinucleotide) and sulfate anion

X-ray diffraction
2.95Å resolution
Source organism: Escherichia coli K-12
Assembly composition:
homo tetramer (preferred)
Entry contents: 1 distinct polypeptide molecule

Assemblies

Assembly 1 (preferred)
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Multimeric state: homo tetramer
Accessible surface area: 44817.95 Å2
Buried surface area: 12979.96 Å2
Dissociation area: 2,199.41 Å2
Dissociation energy (ΔGdiss): 13.82 kcal/mol
Dissociation entropy (TΔSdiss): 15.38 kcal/mol
Symmetry number: 4
PDBe Complex ID: PDB-CPX-141865
Assembly 2
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Multimeric state: homo tetramer
Accessible surface area: 45114.84 Å2
Buried surface area: 12948.89 Å2
Dissociation area: 2,203.58 Å2
Dissociation energy (ΔGdiss): 11.28 kcal/mol
Dissociation entropy (TΔSdiss): 15.39 kcal/mol
Symmetry number: 4
PDBe Complex ID: PDB-CPX-141865
Assembly 3
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Multimeric state: homo tetramer
Accessible surface area: 45462.05 Å2
Buried surface area: 12768.37 Å2
Dissociation area: 2,132.07 Å2
Dissociation energy (ΔGdiss): 11.19 kcal/mol
Dissociation entropy (TΔSdiss): 15.37 kcal/mol
Symmetry number: 4
PDBe Complex ID: PDB-CPX-141865
Assembly 4
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Multimeric state: homo tetramer
Accessible surface area: 45792.59 Å2
Buried surface area: 12735.7 Å2
Dissociation area: 2,082.09 Å2
Dissociation energy (ΔGdiss): 10.9 kcal/mol
Dissociation entropy (TΔSdiss): 15.36 kcal/mol
Symmetry number: 4
PDBe Complex ID: PDB-CPX-141865

Macromolecules

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