› 6mld

X-ray diffraction
1.66Å resolution

Crystal structure of the periplasmic Lysine-, Arginine-, Ornithine-binding protein (LAO) F52A mutant from Salmonella typhimurium

Released:
DOI: 10.2210/pdb6mld/pdb
PDB entry 6mld coloured by chain, front view.
PDB entry 6mld coloured by chain, side view.
PDB entry 6mld coloured by chain, top view.
Source organism: Salmonella enterica subsp. enterica serovar Typhimurium str. LT2
Primary publication:
The interplay of protein-ligand and water-mediated interactions shape affinity and selectivity in the LAO binding protein.
Vergara R, Romero-Romero S, Velázquez-López I, Espinoza-Pérez G, Rodríguez-Hernández A, Pulido NO, Sosa-Peinado A, Rodríguez-Romero A, Fernández-Velasco DA
FEBS J 287 763-782 (2020)
PMID: 31348608

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-136371 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Lysine/arginine/ornithine-binding periplasmic protein Chain: A
Molecule details ›
Chain: A
Length: 238 amino acids
Theoretical weight: 25.98 KDa
Source organism: Salmonella enterica subsp. enterica serovar Typhimurium str. LT2
Expression system: Escherichia coli
UniProt:
  • Canonical: P02911 (Residues: 23-260; Coverage: 100%)
Gene names: STM2355, argT
Sequence domains: Bacterial extracellular solute-binding proteins, family 3

Ligands and Environments

1 bound ligand:
Ligand ACT 4 x ACT
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007 HF
Spacegroup: P212121
Unit cell:
a: 34.758Å b: 76.231Å c: 85.363Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.165 0.161 0.211
Expression system: Escherichia coli

Quick links

Citations

7 citation in other articles

Rosetta design with co-evolutionary information retains protein function.
Schmitz et al. (2021)
6 more

1 mention without citation

The interplay of protein-ligand and water-mediated interactions shape affinity and selectivity in the LAO binding protein.
Vergara et al. (2020)