› 2lbp

X-ray diffraction
2.4Å resolution

STRUCTURE OF THE L-LEUCINE-BINDING PROTEIN REFINED AT 2.4 ANGSTROMS RESOLUTION AND COMPARISON WITH THE LEU(SLASH)ILE(SLASH)VAL-BINDING PROTEIN STRUCTURE

Released:
DOI: 10.2210/pdb2lbp/pdb
PDB entry 2lbp coloured by chain, front view.
PDB entry 2lbp coloured by chain, side view.
PDB entry 2lbp coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Structure of the L-leucine-binding protein refined at 2.4 A resolution and comparison with the Leu/Ile/Val-binding protein structure.
Sack JS, Trakhanov SD, Tsigannik IH, Quiocho FA
J Mol Biol 206 193-207 (1989)
PMID: 2649683

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-138191 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Leucine-specific-binding protein Chain: A
Molecule details ›
Chain: A
Length: 346 amino acids
Theoretical weight: 37.01 KDa
Source organism: Escherichia coli
Expression system: Not provided
UniProt:
  • Canonical: P04816 (Residues: 24-369; Coverage: 100%)
Gene names: JW3423, b3458, livK
Sequence domains: Periplasmic binding protein
Structure domains: Rossmann fold

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P212121
Unit cell:
a: 68.8Å b: 69.34Å c: 74.28Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.213 not available not available
Expression system: Not provided

Quick links

Citations

8 review citations

Modulation of cellular function by polyamines.
Igarashi et al. (2010)
7 more

4 mentions without citation

Computationally designed libraries for rapid enzyme stabilization.
Wijma et al. (2014)
3 more