› 2pfe

X-ray diffraction
1.44Å resolution

Crystal Structure of Thermobifida fusca Protease A (TFPA)

Released:
DOI: 10.2210/pdb2pfe/pdb
PDB entry 2pfe coloured by chain, front view.
PDB entry 2pfe coloured by chain, side view.
PDB entry 2pfe coloured by chain, top view.
Source organism: Thermobifida fusca YX
Primary publication:
Mesophile versus thermophile: insights into the structural mechanisms of kinetic stability.
Kelch BA, Agard DA
J Mol Biol 370 784-95 (2007)
PMID: 17543987

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-175317 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Peptidase S1A alpha-lytic prodomain domain-containing protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 186 amino acids
Theoretical weight: 18.94 KDa
Source organism: Thermobifida fusca YX
Expression system: Streptomyces lividans
UniProt:
  • Canonical: Q47SP5 (Residues: 183-368; Coverage: 55%)
Gene name: Tfu_0484
Structure domains: Trypsin-like serine proteases

Ligands and Environments

3 bound ligands:
Ligand SO4 2 x SO4
Ligand AES 2 x AES
Ligand GOL 2 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.2.2
Spacegroup: C2
Unit cell:
a: 130.959Å b: 68.552Å c: 40.355Å
α: 90° β: 101.98° γ: 90°
R-values:
R R work R free
0.205 0.202 0.229
Expression system: Streptomyces lividans

Quick links

Citations

1 review citation

Protein folding at extreme temperatures: Current issues.
Feller G. (2018)
18 other articles

1 mention without citation

Proteolytic activation of both components of the cation stress-responsive Slt pathway in Aspergillus nidulans.
Mellado et al. (2016)