› 2ock

X-ray diffraction
1.85Å resolution

Crystal structure of valacyclovir hydrolase D123N mutant

Released:
DOI: 10.2210/pdb2ock/pdb
PDB entry 2ock coloured by chain, front view.
PDB entry 2ock coloured by chain, side view.
PDB entry 2ock coloured by chain, top view.
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)
Assembly name:
PDBe Complex ID:
PDB-CPX-567321 (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

2 bound ligands:
Ligand MN 1 x MN
Ligand MG 1 x MG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 32-ID
Spacegroup: P62
Unit cell:
a: 88.989Å b: 88.989Å c: 86.353Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.237 0.237 0.273
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

14 review citations

The metabolic serine hydrolases and their functions in mammalian physiology and disease.
Long et al. (2011)
13 more

1 mention without citation

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