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› 5etj

X-ray diffraction
2.3Å resolution

Crystal structure of purine nucleoside phosphorylase (E258D, L261A) mutant from human complexed with DADMe-ImmG and phosphate

Released:
DOI: 10.2210/pdb5etj/pdb
Model geometry
Fit model/data
PDB entry 5etj coloured by chain, front view.
PDB entry 5etj coloured by chain, side view.
PDB entry 5etj coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Modulating Enzyme Catalysis through Mutations Designed to Alter Rapid Protein Dynamics.
Zoi I, Suarez J, Antoniou D, Cameron SA, Schramm VL, Schwartz SD
J Am Chem Soc 138 3403-9 (2016)
PMID: 26927977

Function and Biology Details

Reaction catalysed: 
(1) a purine D-ribonucleoside + phosphate = a purine nucleobase + alpha-D-ribose 1-phosphate.
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-132560 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Purine nucleoside phosphorylase Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 324 amino acids
Theoretical weight: 36.09 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P00491 (Residues: 1-289; Coverage: 100%)
Gene names: NP, PNP
Sequence domains: Phosphorylase superfamily
Structure domains: Nucleoside phosphorylase domain

Ligands and Environments

2 bound ligands:
Ligand IM5 6 x IM5
Ligand PO4 12 x PO4
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: APS BEAMLINE 31-ID
Spacegroup: C2
Unit cell:
a: 268.808Å b: 58.845Å c: 173.155Å
α: 90° β: 112.92° γ: 90°
R-values:
R R work R free
0.18 0.178 0.211
Expression system: Escherichia coli BL21(DE3)

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Citations

6 review citations

Promoting Vibrations and the Function of Enzymes. Emerging Theoretical and Experimental Convergence.
Schramm et al. (2018)
5 more

1 mention without citation

Modulating Enzyme Catalysis through Mutations Designed to Alter Rapid Protein Dynamics.
Zoi et al. (2016)