X-ray diffraction
1.9Å resolution

Crystal structure of purine nucleoside phosphorylase I from Planctomyces limnophilus DSM 3776, NYSGRC Target 029364.

Entry authors: Malashkevich VN, Bonanno JB, Bhosle R, Toro R, Hillerich B, Gizzi A, Garforth S, Kar A, Chan MK, Lafluer J, Patel H, Matikainen B, Chamala S, Lim S, Celikgil A, Villegas G, Evans B, Love J, Fiser A, Khafizov K, Seidel R, Almo SC, New York Structural Genomics Research Consortium (NYSGRC)

Function and Biology Details

Reaction catalysed:
Purine deoxynucleoside + phosphate = purine + 2'-deoxy-alpha-D-ribose 1-phosphate
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assemblies composition:
homo trimer (preferred)
homo hexamer
Entry contents:
1 distinct polypeptide molecule
Purine nucleoside phosphorylase Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 297 amino acids
Theoretical weight: 32.99 KDa
Source organism: Planctopirus limnophila DSM 3776
Expression system: Escherichia coli BL21(DE3)
  • Canonical: D5SMY7 (Residues: 1-275; Coverage: 100%)
Gene name: Plim_2216
Sequence domains: Phosphorylase superfamily
Structure domains: Nucleoside phosphorylase domain

Ligands and Environments

3 bound ligands:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 31-ID
Spacegroup: P1
Unit cell:
a: 80.95Å b: 81.06Å c: 91.616Å
α: 103.42° β: 105.36° γ: 112.73°
R R work R free
0.215 0.213 0.258
Expression system: Escherichia coli BL21(DE3)