› 2mk5

Solution NMR

Solution structure of a protein domain

Released:
DOI: 10.2210/pdb2mk5/pdb
PDB entry 2mk5 coloured by chain, ensemble of 20 models, front view.
PDB entry 2mk5 coloured by chain, ensemble of 20 models, side view.
PDB entry 2mk5 coloured by chain, ensemble of 20 models, top view.
Source organism: Staphylococcus phage G15
Primary publication:
Structural and biochemical characterization reveals LysGH15 as an unprecedented "EF-hand-like" calcium-binding phage lysin.
Gu J, Feng Y, Feng X, Sun C, Lei L, Ding W, Niu F, Jiao L, Yang M, Li Y, Liu X, Song J, Cui Z, Han D, Du C, Yang Y, Ouyang S, Liu ZJ, Han W
PLoS Pathog 10 e1004109 (2014)
PMID: 24831957

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-112802 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Peptidase C51 domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 131 amino acids
Theoretical weight: 14.05 KDa
Source organism: Staphylococcus phage G15
Expression system: Escherichia coli
UniProt:
  • Canonical: D6QY02 (Residues: 368-495; Coverage: 26%)
Gene names: GH15_071, lysGH15
Sequence domains: Bacterial SH3 domain
Structure domains: SH3 Domains

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 94%
Refinement method: molecular dynamics, simulated annealing
Expression system: Escherichia coli

Quick links

Citations

6 review citations

Cell Wall Hydrolases in Bacteria: Insight on the Diversity of Cell Wall Amidases, Glycosidases and Peptidases Toward Peptidoglycan.
Vermassen et al. (2019)
5 more

5 mentions without citation

Structural and biochemical characterization reveals LysGH15 as an unprecedented "EF-hand-like" calcium-binding phage lysin.
Gu et al. (2014)
4 more