› 5a0n

X-ray diffraction
1.3Å resolution

N-terminal thioester domain of protein F2 like fibronectin-binding protein from Streptococcus pneumoniae

Released:
DOI: 10.2210/pdb5a0n/pdb
PDB entry 5a0n coloured by chain, front view.
PDB entry 5a0n coloured by chain, side view.
PDB entry 5a0n coloured by chain, top view.
Source organism: Streptococcus pneumoniae SP14-BS69
Primary publication:
An internal thioester in a pathogen surface protein mediates covalent host binding.
Walden M, Edwards JM, Dziewulska AM, Bergmann R, Saalbach G, Kan SY, Miller OK, Weckener M, Jackson RJ, Shirran SL, Botting CH, Florence GJ, Rohde M, Banfield MJ, Schwarz-Linek U
Elife 4 (2015)
PMID: 26032562

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-237258 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
PROTEIN F2 LIKE FIBRONECTIN-BINDING PROTEIN Chain: A
Molecule details ›
Chain: A
Length: 220 amino acids
Theoretical weight: 25.81 KDa
Source organism: Streptococcus pneumoniae SP14-BS69
Expression system: Escherichia coli BL21(DE3)

Ligands and Environments

2 bound ligands:
Ligand MES 1 x MES
Ligand GOL 1 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I02
Spacegroup: P41212
Unit cell:
a: 59.86Å b: 59.86Å c: 121.66Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.121 0.119 0.151
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

6 review citations

Engineering of Metabolic Pathways by Artificial Enzyme Channels.
Pröschel et al. (2015)
5 more

3 mentions without citation

An internal thioester in a pathogen surface protein mediates covalent host binding.
Walden et al. (2015)
2 more