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4ODL

Structure of SlyD from Thermus thermophilus in complex with S2 peptide

Summary for 4ODL
Entry DOI10.2210/pdb4odl/pdb
Related4ODK 4ODM 4ODN 4ODO 4ODP 4ODQ 4ODR
DescriptorPeptidyl-prolyl cis-trans isomerase SlyD, 30S ribosomal protein S2, CHLORIDE ION, ... (4 entities in total)
Functional Keywordsfkbp domain, if domain, chaperone, peptidyl-prolyl isomerase, ppiase, isomerase
Biological sourceThermus thermophilus
More
Total number of polymer chains6
Total formula weight42300.28
Authors
Quistgaard, E.M.,Low, C.,Nordlund, P. (deposition date: 2014-01-10, release date: 2015-01-14, Last modification date: 2024-11-20)
Primary citationQuistgaard, E.M.,Weininger, U.,Ural-Blimke, Y.,Modig, K.,Nordlund, P.,Akke, M.,Low, C.
Molecular insights into substrate recognition and catalytic mechanism of the chaperone and FKBP peptidyl-prolyl isomerase SlyD.
BMC Biol., 14:82-82, 2016
Cited by
PubMed Abstract: Peptidyl-prolyl isomerases (PPIases) catalyze cis/trans isomerization of peptidyl-prolyl bonds, which is often rate-limiting for protein folding. SlyD is a two-domain enzyme containing both a PPIase FK506-binding protein (FKBP) domain and an insert-in-flap (IF) chaperone domain. To date, the interactions of these domains with unfolded proteins have remained rather obscure, with structural information on binding to the FKBP domain being limited to complexes involving various inhibitor compounds or a chemically modified tetrapeptide.
PubMed: 27664121
DOI: 10.1186/s12915-016-0300-3
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.916 Å)
Structure validation

243531

数据于2025-10-22公开中

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