› 3u4k

X-ray diffraction
3Å resolution

Crystal structure of the receptor binding domain of plasmid-born adhesin MrkD1P of Klebsiella pneumoniae

Released:
DOI: 10.2210/pdb3u4k/pdb
PDB entry 3u4k coloured by chain, front view.
PDB entry 3u4k coloured by chain, side view.
PDB entry 3u4k coloured by chain, top view.
Source organism: Klebsiella pneumoniae
Primary publication:
Crystal structure of the MrkD1P receptor binding domain of Klebsiella pneumoniae and identification of the human collagen V binding interface.
Rêgo AT, Johnson JG, Gelbel S, Enguita FJ, Clegg S, Waksman G
Mol Microbiol 86 882-93 (2012)
PMID: 22988966

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-149345 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Fimbria adhesin protein Chain: A
Molecule details ›
Chain: A
Length: 185 amino acids
Theoretical weight: 19.45 KDa
Source organism: Klebsiella pneumoniae
Expression system: Escherichia coli
UniProt:
  • Canonical: P21648 (Residues: 21-181; Coverage: 53%)
Gene name: mrkD
Structure domains: Immunoglobulin-like

Ligands and Environments

No bound ligands
1 modified residue:
Ligand MSE 4 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: P3121
Unit cell:
a: 49.813Å b: 49.813Å c: 169.933Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.229 0.227 0.273
Expression system: Escherichia coli

Quick links

Citations

2 review citations

The molecular dissection of the chaperone-usher pathway.
Geibel et al. (2014)
1 more

1 mention without citation

Structure-function correlates of fibrinogen binding by Acinetobacter adhesins critical in catheter-associated urinary tract infections.
Tamadonfar et al. (2023)