› 1mt3

X-ray diffraction
2Å resolution

Crystal Structure of the Tricorn Interacting Factor Selenomethionine-F1

Released:
DOI: 10.2210/pdb1mt3/pdb
PDB entry 1mt3 coloured by chain, front view.
PDB entry 1mt3 coloured by chain, side view.
PDB entry 1mt3 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: 33.95 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

1 bound ligand:
Ligand MES 1 x MES
1 modified residue:
Ligand MSE 9 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: MPG/DESY, HAMBURG BEAMLINE BW6
Spacegroup: P212121
Unit cell:
a: 51.968Å b: 60.759Å c: 80.678Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.285 0.255 0.28
Expression system: Escherichia coli

Quick links

Citations

1 review citation

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

1 mention without citation

Structure of XC6422 from Xanthomonas campestris at 1.6 A resolution: a small serine alpha/beta-hydrolase.
Yang et al. (2006)