› 1mu0

X-ray diffraction
2.4Å resolution

Crystal Structure of the Tricorn Interacting Factor F1 Complex with PCK

Released:
DOI: 10.2210/pdb1mu0/pdb
PDB entry 1mu0 coloured by chain, front view.
PDB entry 1mu0 coloured by chain, side view.
PDB entry 1mu0 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

1 bound ligand:
Ligand PHK 1 x PHK
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU300
Spacegroup: P212121
Unit cell:
a: 57.579Å b: 61.721Å c: 80.435Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.366 0.314 0.366
Expression system: Escherichia coli

Quick links

Citations

1 review citation

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

4 mentions without citation

Towards the prediction of protein interaction partners using physical docking.
Wass et al. (2011)
3 more