Structure analysis

Crystal Structure of ADP ribose phosphatase of NSP3 from SARS CoV-2 in the complex with ADP ribose

X-ray diffraction
1.5Å resolution
Assembly composition:
monomeric (preferred)
Entry contents: 1 distinct polypeptide molecule

Assemblies

Assembly 1 (preferred)
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Multimeric state: monomeric

Binding statistics and energies are not available for this assembly
Assembly 2
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Multimeric state: monomeric
Accessible surface area: 7600 Å2
Buried surface area: 1000 Å2
Dissociation area: 500 Å2
Dissociation energy (ΔGdiss): 11 kcal/mol
Dissociation entropy (TΔSdiss): 6 kcal/mol
Interface energy (ΔGint): -11 kcal/mol
Symmetry number: 1

Macromolecules

Chains: A, B
Length: 170 amino acids
Theoretical weight: 18.28 KDa
Source organism: Severe acute respiratory syndrome coronavirus 2
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P0DTD1 (Residues: 1024-1192; Coverage: 2%)
Gene names: 1a-1b, rep
Pfam: Macro domain

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