› 5uue

X-ray diffraction
1.6Å resolution

Tetragonal thermolysin cryocooled to 100 K with 50% methanol as cryoprotectant

Released:
DOI: 10.2210/pdb5uue/pdb
PDB entry 5uue coloured by chain, front view.
PDB entry 5uue coloured by chain, side view.
PDB entry 5uue coloured by chain, top view.
Source organism: Bacillus thermoproteolyticus
Primary publication:
The impact of cryosolution thermal contraction on proteins and protein crystals: volumes, conformation and order.
Juers DH, Farley CA, Saxby CP, Cotter RA, Cahn JKB, Holton-Burke RC, Harrison K, Wu Z
Acta Crystallogr D Struct Biol 74 922-938 (2018)
PMID: 30198901

Function and Biology Details

Reaction catalysed: 
Preferential cleavage: -|-Leu > -|-Phe.
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-133580 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Thermolysin Chain: A
Molecule details ›
Chain: A
Length: 316 amino acids
Theoretical weight: 34.36 KDa
Source organism: Bacillus thermoproteolyticus
Expression system: Bacillus thermoproteolyticus
UniProt:
  • Canonical: P00800 (Residues: 233-548; Coverage: 61%)
Gene name: npr
Sequence domains:
Structure domains:

Ligands and Environments

4 bound ligands:
Ligand CA 3 x CA
Ligand ZN 6 x ZN
Ligand CL 4 x CL
Ligand MOH 8 x MOH
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: OXFORD DIFFRACTION ENHANCE ULTRA
Spacegroup: P41212
Unit cell:
a: 96.149Å b: 96.149Å c: 104.8Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.202 0.201 0.235
Expression system: Bacillus thermoproteolyticus

Quick links

Citations

3 citation in other articles

The low-cost Shifter microscope stage transforms the speed and robustness of protein crystal harvesting.
Wright et al. (2021)
2 more

1 mention without citation

The impact of cryosolution thermal contraction on proteins and protein crystals: volumes, conformation and order.
Juers et al. (2018)