› 1mtz

X-ray diffraction
1.8Å resolution

Crystal Structure of the Tricorn Interacting Factor F1

Released:
DOI: 10.2210/pdb1mtz/pdb
PDB entry 1mtz coloured by chain, front view.
PDB entry 1mtz coloured by chain, side view.
PDB entry 1mtz coloured by chain, top view.
Source organism: Thermoplasma acidophilum
Primary publication:
Structures of the tricorn-interacting aminopeptidase F1 with different ligands explain its catalytic mechanism.
Goettig P, Groll M, Kim JS, Huber R, Brandstetter H
EMBO J 21 5343-52 (2002)
PMID: 12374735

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-161192 (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: alpha/beta hydrolase fold
Structure domains: alpha/beta hydrolase

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

Quick links

Citations

1 review citation

Molecular machines for protein degradation.
Groll et al. (2005)
25 other articles

3 mentions without citation

The proteolytic system of lactic acid bacteria revisited: a genomic comparison.
Liu et al. (2010)
2 more