› 2pnl

X-ray diffraction
2.21Å resolution

Crystal structure of VP4 protease from infectious pancreatic necrosis virus (IPNV) in space group P1

Released:
DOI: 10.2210/pdb2pnl/pdb
PDB entry 2pnl coloured by chain, front view.
PDB entry 2pnl coloured by chain, side view.
PDB entry 2pnl coloured by chain, top view.
Source organism: Infectious pancreatic necrosis virus
Primary publication:
Crystal structure of the VP4 protease from infectious pancreatic necrosis virus reveals the acyl-enzyme complex for an intermolecular self-cleavage reaction.
Lee J, Feldman AR, Delmas B, Paetzel M
J Biol Chem 282 24928-37 (2007)
PMID: 17553791

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-106740 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
PP Chains: A, B, C, D, E, F, G, H, I, J
Molecule details ›
Chains: A, B, C, D, E, F, G, H, I, J
Length: 203 amino acids
Theoretical weight: 21.76 KDa
Source organism: Infectious pancreatic necrosis virus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: A1XQQ8 (Residues: 514-716; Coverage: 21%)
Sequence domains: Birnavirus VP4 protein
Structure domains: Ribosomal Protein S5; domain 2

Ligands and Environments

1 bound ligand:
Ligand GAI 17 x GAI
1 modified residue:
Ligand MSE 30 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X8C
Spacegroup: P1
Unit cell:
a: 41.703Å b: 69.262Å c: 191.388Å
α: 93.06° β: 95.03° γ: 97.56°
R-values:
R R work R free
0.2 0.19 0.267
Expression system: Escherichia coli BL21(DE3)

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Citations

2 review citations

The penicillin-binding proteins: structure and role in peptidoglycan biosynthesis.
Sauvage et al. (2008)
1 more

3 mentions without citation

Structure of the catalytic domain of the human mitochondrial Lon protease: proposed relation of oligomer formation and activity.
García-Nafría et al. (2010)
2 more