› 1xqw

X-ray diffraction
2Å resolution

Crystal structure of F1-mutant S105A complex with PHE-LEU

Released:
DOI: 10.2210/pdb1xqw/pdb
PDB entry 1xqw coloured by chain, front view.
PDB entry 1xqw coloured by chain, side view.
PDB entry 1xqw coloured by chain, top view.
Source organism: Thermoplasma acidophilum
Primary publication:
X-ray snapshots of peptide processing in mutants of tricorn-interacting factor F1 from Thermoplasma acidophilum.
Goettig P, Brandstetter H, Groll M, Göhring W, Konarev PV, Svergun DI, Huber R, Kim JS
J Biol Chem 280 33387-96 (2005)
PMID: 15994304

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 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: 33.51 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

2 bound ligands:
Ligand PHE 2 x PHE
Ligand LEU 2 x LEU
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MPG/DESY, HAMBURG BEAMLINE BW6
Spacegroup: P212121
Unit cell:
a: 57.35Å b: 61.88Å c: 80.5Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.265 0.248 0.285
Expression system: Escherichia coli

Quick links

Citations

3 review citations

X-ray solution scattering (SAXS) combined with crystallography and computation: defining accurate macromolecular structures, conformations and assemblies in solution.
Putnam et al. (2007)
2 more

2 mentions without citation

How the Same Core Catalytic Machinery Catalyzes 17 Different Reactions: the Serine-Histidine-Aspartate Catalytic Triad of α/β-Hydrolase Fold Enzymes.
Rauwerdink et al. (2015)
1 more