› 2oci

X-ray diffraction
1.9Å resolution

Crystal structure of valacyclovir hydrolase complexed with a product analogue

Released:
DOI: 10.2210/pdb2oci/pdb
PDB 2oci coloured by chain and viewed from the front.
PDB 2oci coloured by chain and viewed from the side.
PDB 2oci coloured by chain and viewed from the top.
Source organism: Homo sapiens
Primary publication:
Molecular basis of prodrug activation by human valacyclovirase, an alpha-amino acid ester hydrolase.
Lai L, Xu Z, Zhou J, Lee KD, Amidon GL
J. Biol. Chem. 283 9318-27 (2008)
PMID: 18256025

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Valacyclovir hydrolase Chain: A
Molecule details ›
Chain: A
Length: 254 amino acids
Theoretical weight: 28.87 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q86WA6 (Residues: 38-291; Coverage: 100%)
Gene names: BPHL, MCNAA
Sequence domains: alpha/beta hydrolase fold
Structure domains: alpha/beta hydrolase

Ligands and Environments

3 bound ligands:
Ligand MN 1 x MN
Ligand MG 1 x MG
Ligand TYC 1 x TYC
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 23-ID-D
Spacegroup: P62
Unit cell:
a: 88.6Å b: 88.6Å c: 86.71Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.196 0.196 0.217
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

13 review citations

Current Drugs to Treat Infections with Herpes Simplex Viruses-1 and -2.
Sadowski et al. (2021)
12 more

4 mentions without citation

Molecular basis of prodrug activation by human valacyclovirase, an alpha-amino acid ester hydrolase.
Lai et al. (2008)
3 more