Assemblies
Assembly Name:
D-erythrose-4-phosphate dehydrogenase
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 Name:
D-erythrose-4-phosphate dehydrogenase
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 Name:
D-erythrose-4-phosphate dehydrogenase
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 Name:
D-erythrose-4-phosphate dehydrogenase
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
Chains: A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P
Length: 338 amino acids
Theoretical weight: 37.22 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli K-12
UniProt:
Pfam:
Length: 338 amino acids
Theoretical weight: 37.22 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli K-12
UniProt:
- Canonical: P0A9B6 (Residues: 2-339; Coverage: 100%)
Pfam:
- Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain
- Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain
- D-erythrose-4-phosphate dehydrogenase
- Glyceraldehyde/Erythrose phosphate dehydrogenase family
- NAD(P)-binding domain superfamily
- Glyceraldehyde 3-phosphate dehydrogenase, NAD(P) binding domain
- Glyceraldehyde 3-phosphate dehydrogenase, active site
- Glyceraldehyde 3-phosphate dehydrogenase, catalytic domain