› 5g59

X-ray diffraction
1.61Å resolution

Structure of the Pyrococcus Furiosus Esterase Pf2001 with space group P3121

Released:
DOI: 10.2210/pdb5g59/pdb
PDB entry 5g59 coloured by chain, front view.
PDB entry 5g59 coloured by chain, side view.
PDB entry 5g59 coloured by chain, top view.
Source organism: Pyrococcus furiosus
Primary publication:
Structural Mechanism for the Temperature-Dependent Activation of the Hyperthermophilic Pf2001 Esterase.
Varejão N, De-Andrade RA, Almeida RV, Anobom CD, Foguel D, Reverter D
Structure 26 199-208.e3 (2018)
PMID: 29307486

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-186329 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Serine aminopeptidase S33 domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 275 amino acids
Theoretical weight: 31.76 KDa
Source organism: Pyrococcus furiosus
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q8TZJ1 (Residues: 21-288; Coverage: 93%)
Gene name: PF2001
Sequence domains: Serine aminopeptidase, S33

Ligands and Environments

1 bound ligand:
Ligand HG 2 x HG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALBA BEAMLINE XALOC
Spacegroup: P3121
Unit cell:
a: 105.334Å b: 105.334Å c: 47.843Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.168 0.167 0.194
Expression system: Escherichia coli BL21

Quick links

Citations

6 citation in other articles

Contribution of the Oligomeric State to the Thermostability of Isoenzyme 3 from Candida rugosa.
Álvarez-Cao et al. (2018)
5 more

4 mentions without citation

Dissecting the Effect of Temperature on Hyperthermophilic Pf2001 Esterase Dimerization by Molecular Dynamics.
Zhang et al. (2023)
3 more