› 4dq5

X-ray diffraction
1.4Å resolution

Structural Investigation of Bacteriophage Phi6 Lysin (WT)

Released:
DOI: 10.2210/pdb4dq5/pdb
PDB entry 4dq5 coloured by chain, front view.
PDB entry 4dq5 coloured by chain, side view.
PDB entry 4dq5 coloured by chain, top view.
Source organism: Pseudomonas virus phi6
Primary publication:
Selective pressure causes an RNA virus to trade reproductive fitness for increased structural and thermal stability of a viral enzyme.
Dessau M, Goldhill D, McBride R, McBride RL, Turner PE, Modis Y
PLoS Genet 8 e1003102 (2012)
PMID: 23209446

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-173313 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
p5 Chains: A, B
Molecule details ›
Chains: A, B
Length: 173 amino acids
Theoretical weight: 19.04 KDa
Source organism: Pseudomonas virus phi6
Expression system: Escherichia coli
UniProt:
  • Canonical: Q283U5 (Residues: 48-220; Coverage: 79%)
Gene names: P5a, p5a
Sequence domains: Peptidase U40
Structure domains: Peptidase U40

Ligands and Environments

1 bound ligand:
Ligand AES 2 x AES
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X29A
Spacegroup: P212121
Unit cell:
a: 62.159Å b: 68.785Å c: 90.045Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.166 0.164 0.177
Expression system: Escherichia coli

Quick links

Citations

7 review citations

Quantifying and understanding the fitness effects of protein mutations: Laboratory versus nature.
Boucher et al. (2016)
6 more

2 mentions without citation

Selective pressure causes an RNA virus to trade reproductive fitness for increased structural and thermal stability of a viral enzyme.
Dessau et al. (2012)
1 more