› 1hz5

X-ray diffraction
1.8Å resolution

CRYSTAL STRUCTURES OF THE B1 DOMAIN OF PROTEIN L FROM PEPTOSTREPTOCOCCUS MAGNUS, WITH A TYROSINE TO TRYPTOPHAN SUBSTITUTION

Released:
DOI: 10.2210/pdb1hz5/pdb
PDB entry 1hz5 coloured by chain, front view.
PDB entry 1hz5 coloured by chain, side view.
PDB entry 1hz5 coloured by chain, top view.
Source organism: Finegoldia magna ATCC 29328
Primary publication:
Structures of the B1 domain of protein L from Peptostreptococcus magnus with a tyrosine to tryptophan substitution.
O'Neill JW, Kim DE, Baker D, Zhang KY
Acta Crystallogr D Biol Crystallogr 57 480-7 (2001)
PMID: 11264576

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domain:
Structure domain:

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-175983 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Gram-positive cocci surface proteins LPxTG domain-containing protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 72 amino acids
Theoretical weight: 8.05 KDa
Source organism: Finegoldia magna ATCC 29328
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q51912 (Residues: 111-173; Coverage: 9%)
Sequence domains: Protein L b1 domain
Structure domains: Ubiquitin-like (UB roll)

Ligands and Environments

1 bound ligand:
Ligand ZN 10 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P3221
Unit cell:
a: 66.437Å b: 66.437Å c: 109.181Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.188 0.188 0.193
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 review citation

3D domain swapping: as domains continue to swap.
Liu et al. (2002)
31 other articles

12 mentions without citation

Selection of optimal variants of Gō-like models of proteins through studies of stretching.
Sułkowska et al. (2008)
11 more