› 5lcn

X-ray diffraction
2.6Å resolution

STRUCTURE OF THE PYROCOCCUS FURIOSUS ESTERASE PF2001 WITH SPACE GROUP P212121

Released:
DOI: 10.2210/pdb5lcn/pdb
PDB entry 5lcn coloured by chain, front view.
PDB entry 5lcn coloured by chain, side view.
PDB entry 5lcn coloured by chain, top view.
Source organism: Pyrococcus furiosus DSM 3638
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:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-186330 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Serine aminopeptidase S33 domain-containing protein Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 275 amino acids
Theoretical weight: 31.76 KDa
Source organism: Pyrococcus furiosus DSM 3638
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8TZJ1 (Residues: 14-14, 21-288; Coverage: 93%)
Gene name: PF2001
Sequence domains: Serine aminopeptidase, S33

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: ALBA BEAMLINE XALOC
Spacegroup: P212121
Unit cell:
a: 96.495Å b: 99.44Å c: 146.049Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.199 0.196 0.256
Expression system: Escherichia coli

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Citations

7 citation in other articles

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