› 4odo

X-ray diffraction
1.6Å resolution

Structure of SlyD from Thermus thermophilus in complex with FK506

Released:
DOI: 10.2210/pdb4odo/pdb
PDB entry 4odo coloured by chain, front view.
PDB entry 4odo coloured by chain, side view.
PDB entry 4odo coloured by chain, top view.
Source organism: Thermus thermophilus
Primary publication:
Molecular insights into substrate recognition and catalytic mechanism of the chaperone and FKBP peptidyl-prolyl isomerase SlyD.
Quistgaard EM, Weininger U, Ural-Blimke Y, Modig K, Nordlund P, Akke M, Löw C
BMC Biol 14 82 (2016)
PMID: 27664121

Function and Biology Details

Reaction catalysed: 
Peptidylproline (omega=180) = peptidylproline (omega=0)
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-178159 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Peptidyl-prolyl cis-trans isomerase Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 158 amino acids
Theoretical weight: 17.4 KDa
Source organism: Thermus thermophilus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q5SLE7 (Residues: 1-149; Coverage: 100%)
Gene name: TTHA0346
Sequence domains: FKBP-type peptidyl-prolyl cis-trans isomerase
Structure domains: Chitinase A; domain 3

Ligands and Environments

5 bound ligands:
Ligand MG 4 x MG
Ligand CL 3 x CL
Ligand FK5 3 x FK5
Ligand BTB 1 x BTB
Ligand GOL 1 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I24
Spacegroup: P1
Unit cell:
a: 48.71Å b: 50.21Å c: 57.67Å
α: 85.74° β: 68.92° γ: 80.12°
R-values:
R R work R free
0.181 0.18 0.204
Expression system: Escherichia coli

Quick links

Citations

10 citation in other articles

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Lauber et al. (2018)
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3 mentions without citation

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Doria-Rose et al. (2014)
2 more