Structure analysis

Crystal Structure of N-Succinylarginine Dihydrolase, AstB, bound to Substrate and Product, an Enzyme from the Arginine Catabolic Pathway of Escherichia coli

X-ray diffraction
2.2Å resolution
Source organism: Escherichia coli
Assembly composition:
homo dimer (preferred)
Entry contents: 1 distinct polypeptide molecule

Assemblies

Assembly 1 (preferred)
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Multimeric state: homo dimer

Binding statistics and energies are not available for this assembly
Assembly 2
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Multimeric state: homo dimer
Accessible surface area: 30600 Å2
Buried surface area: 3500 Å2
Dissociation area: 300 Å2
Dissociation energy (ΔGdiss): 1 kcal/mol
Dissociation entropy (TΔSdiss): 4 kcal/mol
Interface energy (ΔGint): -211 kcal/mol
Symmetry number: 1

Macromolecules

Chains: A, B, C, D
Length: 458 amino acids
Theoretical weight: 50.54 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P76216 (Residues: 2-447; Coverage: 100%)
Gene names: JW1734, astB, b1745, ydjT
Pfam: Succinylarginine dihydrolase
InterPro:
CATH: Succinylarginine dihydrolase
SCOP: Succinylarginine dihydrolase-like

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