› 2as9

X-ray diffraction
1.7Å resolution

Functional and structural characterization of Spl proteases from staphylococcus aureus

Released:
DOI: 10.2210/pdb2as9/pdb
PDB entry 2as9 coloured by chain, front view.
PDB entry 2as9 coloured by chain, side view.
PDB entry 2as9 coloured by chain, top view.
Source organism: Staphylococcus aureus
Primary publication:
Functional and structural characterization of Spl proteases from Staphylococcus aureus.
Popowicz GM, Dubin G, Stec-Niemczyk J, Czarny A, Dubin A, Potempa J, Holak TA
J Mol Biol 358 270-9 (2006)
PMID: 16516230

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-557830 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Serine protease SplC Chains: A, B
Molecule details ›
Chains: A, B
Length: 210 amino acids
Theoretical weight: 23.38 KDa
Source organism: Staphylococcus aureus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q2FXC4 (Residues: 37-239; Coverage: 100%)
Gene names: SAOUHSC_01939, splC
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases

Ligands and Environments

1 bound ligand:
Ligand ZN 7 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MPG/DESY, HAMBURG BEAMLINE BW6
Spacegroup: P212121
Unit cell:
a: 53.12Å b: 81.4Å c: 107.39Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.215 0.211 0.243
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

7 review citations

Staphylococcus aureus Secreted Toxins and Extracellular Enzymes.
Tam et al. (2019)
6 more

7 mentions without citation

Lysine carboxylation: unveiling a spontaneous post-translational modification.
Jimenez-Morales et al. (2014)
6 more