Structure analysis

Crystal structure of human PNP complexed with MESG

X-ray diffraction
2.8Å resolution
Source organism: Homo sapiens
Assemblies composition:
monomeric (preferred)
homo trimer
Entry contents: 1 distinct polypeptide molecule

Assemblies

Assembly 1 (preferred)
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Multimeric state: monomeric
Accessible surface area: 12037.66 Å2
Buried surface area: 1279.31 Å2
Dissociation area: 355.48 Å2
Dissociation energy (ΔGdiss): 3.03 kcal/mol
Dissociation entropy (TΔSdiss): 4.07 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-132559
Assembly 2
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Multimeric state: homo trimer
Accessible surface area: 28473.68 Å2
Buried surface area: 11465.89 Å2
Dissociation area: 3,884.27 Å2
Dissociation energy (ΔGdiss): 50.35 kcal/mol
Dissociation entropy (TΔSdiss): 27.71 kcal/mol
Symmetry number: 3
PDBe Complex ID: PDB-CPX-132560

Macromolecules

Chain: E
Length: 289 amino acids
Theoretical weight: 32.18 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P00491 (Residues: 1-289; Coverage: 100%)
Gene names: NP, PNP
Pfam: Phosphorylase superfamily
InterPro:
CATH: Nucleoside phosphorylase domain
SCOP: Purine and uridine phosphorylases

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