4ODK: SlyD from Thermus thermophilus

Structure of SlyD from Thermus thermophilus in complex with T1 peptide. Determined by X-ray diffraction at 1.4 Å resolution. Released 14 Jan 2015.

Method
X-ray diffraction
Resolution
1.4 Å
Organisms
Thermus thermophilus, Aspergillus oryzae
Chains
3
Atoms
1,527
Mol. weight
20.89 kDa
Released
14 Jan 2015

Explore 4ODK in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4ODK contains 9 α-helices and 12 β-strands across 2 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 9 helices, 11 β-strands

ElementResiduesLengthSheet
β-strand211
β-strand7-17112
β-strand20-30112
α-helix38-447
α-helix471
β-strand4811
β-strand52-5762
α-helix59-613
α-helix65-673
α-helix68-703
β-strand71-7553
α-helix76-783
β-strand90-9453
β-strand100-109103
β-strand112-11653
β-strand126-137122
α-helix138-1392
α-helix140-1456
α-helix148-1503
β-strand154-15522
Chain B: 0 helices, 1 β-strand
ElementResiduesLengthSheet
β-strand7213

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Peptidyl-prolyl cis-trans isomerase SlyDAprotein158Thermus thermophilusQ5SLE7 (AlphaFold model)
Guanyl-specific ribonuclease T1B, Cprotein16Aspergillus oryzaeP00651 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>4ODK_1 Peptidyl-prolyl cis-trans isomerase SlyD (chains A)
MKVGQDKVVTIRYTLQVEGEVLDQGELSYLHGHRNLIPGLEEALEGREEGEAFQAHVPAE
KAYGPHDPEGVQVVPLSAFPEDAEVVPGAQFYAQDMEGNPMPLTVVAVEGEEVTVDFNHP
LAGKDLDFQVEVVKVREATPEELLHGHAHPSGHHHHHH
Sequence of entity 2 (B, C), FASTA
>4ODK_2 Guanyl-specific ribonuclease T1 (chains B, C)
VGSNSYPHKYNNYEGX

Primary citation

Molecular insights into substrate recognition and catalytic mechanism of the chaperone and FKBP peptidyl-prolyl isomerase SlyD. Quistgaard, E.M., Weininger, U., Ural-Blimke, Y. et al. BMC Biol (2016) 14:82-82. DOI 10.1186/s12915-016-0300-3 · PubMed

Other PDB entries of the same protein (UniProt Q5SLE7 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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