› 4odq

X-ray diffraction
2Å resolution

Structure of SlyD delta-IF from Thermus thermophilus in complex with S3 peptide

Released:
DOI: 10.2210/pdb4odq/pdb
PDB entry 4odq coloured by chain, front view.
PDB entry 4odq coloured by chain, side view.
PDB entry 4odq coloured by chain, top view.
Source organisms:
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:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-141630 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Peptidyl-prolyl cis-trans isomerase; Peptidyl-prolyl cis-trans isomerase FKBP1A Chain: A
Molecule details ›
Chain: A
Length: 110 amino acids
Theoretical weight: 12.18 KDa
Source organisms: Expression system: Escherichia coli
UniProt:
  • Canonical: Q5SLE7 (Residues: 1-64, 127-149; Coverage: 58%)
  • Canonical: P62942 (Residues: 85-98; Coverage: 13%)
Gene names: FKBP1, FKBP12, FKBP1A, TTHA0346
Sequence domains: FKBP-type peptidyl-prolyl cis-trans isomerase
Structure domains: Chitinase A; domain 3
Small ribosomal subunit protein uS3 Chain: B
Molecule details ›
Chain: B
Length: 16 amino acids
Theoretical weight: 1.79 KDa
Source organism: Escherichia coli K-12
Expression system: Not provided
UniProt:
  • Canonical: P0A7V3 (Residues: 11-25; Coverage: 6%)
Gene names: JW3276, b3314, rpsC

Ligands and Environments

3 bound ligands:
Ligand CL 1 x CL
Ligand CA 4 x CA
Ligand NI 1 x NI
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SOLEIL BEAMLINE PROXIMA 1
Spacegroup: P4132
Unit cell:
a: 93.56Å b: 93.56Å c: 93.56Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.195 0.194 0.213
Expression systems:
  • Escherichia coli
  • Not provided

Quick links

Citations

11 citation in other articles

Type 9 secretion system structures reveal a new protein transport mechanism.
Lauber et al. (2018)
10 more

1 mention without citation

Molecular insights into substrate recognition and catalytic mechanism of the chaperone and FKBP peptidyl-prolyl isomerase SlyD.
Quistgaard et al. (2016)