1mtz

X-ray diffraction
1.8Å resolution

Crystal Structure of the Tricorn Interacting Factor F1

Released:

Function and Biology Details

Reaction catalysed:
Release of N-terminal proline from a peptide.
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Proline iminopeptidase Chain: A
Molecule details ›
Chain: A
Length: 293 amino acids
Theoretical weight: 33.53 KDa
Source organism: Thermoplasma acidophilum
Expression system: Escherichia coli
UniProt:
  • Canonical: P96084 (Residues: 1-293; Coverage: 100%)
Gene names: Ta0830, pip
Sequence domains: Serine aminopeptidase, S33
Structure domains: Rossmann fold

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06SA
Spacegroup: P212121
Unit cell:
a: 54.961Å b: 57.095Å c: 82.274Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.236 0.199 0.236
Expression system: Escherichia coli