4wr2

X-ray diffraction
1.7Å resolution

Crystal structure of a putative pyrimidine-specific ribonucleoside hydrolase (RihA) Protein from Shewanella loihica PV-4 (SHEW_0697, Target PSI-029635) with divalent cation and PEG 400 bound at the active site

Released:
Source organism: Shewanella loihica PV-4
Entry authors: Himmel DM, 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, Seidel RD, Bonanno JB, Almo SC, New York Structural Genomics Research Consortium (NYSGRC)

Function and Biology Details

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Pyrimidine-specific ribonucleoside hydrolase RihA Chain: A
Molecule details ›
Chain: A
Length: 335 amino acids
Theoretical weight: 36.54 KDa
Source organism: Shewanella loihica PV-4
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: A3QAS1 (Residues: 1-335; Coverage: 100%)
Gene names: Shew_0697, rihA
Sequence domains: Inosine-uridine preferring nucleoside hydrolase
Structure domains: Ribonucleoside hydrolase-like

Ligands and Environments

2 bound ligands:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 31-ID
Spacegroup: I222
Unit cell:
a: 60.078Å b: 115.047Å c: 141.64Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.157 0.157 0.171
Expression system: Escherichia coli BL21(DE3)