Structure analysis

STRUCTURE AND CATALYTIC MECHANISM OF GLUCOSAMINE 6-PHOSPHATE DEAMINASE FROM ESCHERICHIA COLI AT 2.1 ANGSTROMS RESOLUTION

X-ray diffraction
2.1Å resolution
Source organism: Escherichia coli
Assemblies composition:
homo hexamer
homo trimer (preferred)
Entry contents: 1 distinct polypeptide molecule

Assemblies

Assembly 1
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Multimeric state: homo hexamer
Accessible surface area: 61430.14 Å2
Buried surface area: 13571.82 Å2
Dissociation area: 1,652.74 Å2
Dissociation energy (ΔGdiss): 14.8 kcal/mol
Dissociation entropy (TΔSdiss): 15.41 kcal/mol
Symmetry number: 6
PDBe Complex ID: PDB-CPX-141540
Assembly 2 (preferred)
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Multimeric state: homo trimer
Accessible surface area: 32478.54 Å2
Buried surface area: 4996.03 Å2
Dissociation area: 1,907.56 Å2
Dissociation energy (ΔGdiss): 22.86 kcal/mol
Dissociation entropy (TΔSdiss): 26.93 kcal/mol
Symmetry number: 3
PDBe Complex ID: PDB-CPX-141539
Assembly 3
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Multimeric state: homo trimer
Accessible surface area: 32257.08 Å2
Buried surface area: 5270.31 Å2
Dissociation area: 2,056.75 Å2
Dissociation energy (ΔGdiss): 17.9 kcal/mol
Dissociation entropy (TΔSdiss): 26.96 kcal/mol
Symmetry number: 3
PDBe Complex ID: PDB-CPX-141539

Macromolecules

Chains: A, B
Length: 266 amino acids
Theoretical weight: 29.81 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P0A759 (Residues: 1-266; Coverage: 100%)
Gene names: JW0664, b0678, glmD, nagB
Pfam: Glucosamine-6-phosphate isomerases/6-phosphogluconolactonase
InterPro:
CATH: Rossmann fold
SCOP: NagB-like

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