› 1xqy

X-ray diffraction
3.2Å resolution

Crystal structure of F1-mutant S105A complex with PRO-LEU-GLY-GLY

Released:
DOI: 10.2210/pdb1xqy/pdb
Model geometry
Fit model/data
PDB entry 1xqy coloured by chain, front view.
PDB entry 1xqy coloured by chain, side view.
PDB entry 1xqy 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:
Sequence domains:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-161193 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
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
PLGG Chain: Q
Molecule details ›
Chain: Q
Length: 4 amino acids
Theoretical weight: 342 Da
Source organism: Thermoplasma acidophilum
Expression system: Not provided

Ligands and Environments

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

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: RIGAKU RU300
Spacegroup: P212121
Unit cell:
a: 54.17Å b: 60.83Å c: 80.24Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.285 0.268 0.353
Expression systems:
  • Escherichia coli
  • Not provided

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

Proteolytic systems of archaea: slicing, dicing, and mincing in the extreme.
Maupin-Furlow JA. (2018)
1 more