› 1vmk

X-ray diffraction
2.01Å resolution

Crystal structure of Purine nucleoside phosphorylase (TM1596) from Thermotoga maritima at 2.01 A resolution

Released:
DOI: 10.2210/pdb1vmk/pdb
PDB entry 1vmk coloured by chain, front view.
PDB entry 1vmk coloured by chain, side view.
PDB entry 1vmk coloured by chain, top view.
Source organism: Thermotoga maritima MSB8
Entry author: Joint Center for Structural Genomics (JCSG)

Function and Biology Details

Reaction catalysed: 
Purine deoxynucleoside + phosphate = purine + 2'-deoxy-alpha-D-ribose 1-phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-194834 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Purine nucleoside phosphorylase Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 277 amino acids
Theoretical weight: 30.67 KDa
Source organism: Thermotoga maritima MSB8
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9X1T2 (Residues: 1-265; Coverage: 100%)
Gene name: TM_1596
Sequence domains: Phosphorylase superfamily
Structure domains: Nucleoside phosphorylase domain

Ligands and Environments

2 bound ligands:
Ligand GUN 3 x GUN
Ligand MG 1 x MG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-BM
Spacegroup: P1
Unit cell:
a: 46.478Å b: 74.601Å c: 74.591Å
α: 117.34° β: 100.95° γ: 100.71°
R-values:
R R work R free
0.206 0.204 0.24
Expression system: Escherichia coli

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