4ODM: SlyD from Thermus thermophilus

Structure of SlyD from Thermus thermophilus in complex with S2-W23A peptide. Determined by X-ray diffraction at 1.75 Å resolution. Released 14 Jan 2015.

Method
X-ray diffraction
Resolution
1.75 Å
Organisms
Thermus thermophilus, Escherichia coli
Chains
13
Atoms
6,039
Mol. weight
83.14 kDa
Released
14 Jan 2015

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

Secondary structure: helices and β-sheets

4ODM contains 40 α-helices and 52 β-strands across 12 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.

Chains A and B: 8 helices, 11 β-strands

ElementResiduesLengthSheet
β-strand211
β-strand7-17112
β-strand20-30112
β-strand3613
α-helix38-447
α-helix471
β-strand4811
β-strand52-5762
α-helix59-613
α-helix65-673
α-helix68-703
β-strand71-7554
α-helix76-783
β-strand90-9454
β-strand100-109104
β-strand112-11654
β-strand126-137122
α-helix138-1392
α-helix140-1456
Chain C: 9 helices, 11 β-strands
ElementResiduesLengthSheet
β-strand219
β-strand7-171110
β-strand20-301110
β-strand36111
α-helix38-447
α-helix471
β-strand4819
β-strand52-57610
α-helix59-613
α-helix65-673
α-helix68-703
β-strand71-75512
α-helix76-783
β-strand90-94512
β-strand100-1091012
β-strand112-116512
β-strand126-1371210
α-helix138-1392
α-helix140-1456
α-helix148-1503
Chain D: 9 helices, 11 β-strands
ElementResiduesLengthSheet
β-strand2113
β-strand7-171114
β-strand20-301114
β-strand36115
α-helix38-447
α-helix471
β-strand48113
β-strand52-57614
α-helix59-613
α-helix65-673
α-helix68-703
β-strand71-75516
α-helix76-783
α-helix801
β-strand90-94516
β-strand100-1091016
β-strand112-116516
β-strand126-1371214
α-helix138-1392
α-helix140-1456
Chains E, G and I: 0 helices, 1 β-strand
ElementResiduesLengthSheet
β-strand2813
Chains F and J: 1 helix, 1 β-strand
ElementResiduesLengthSheet
α-helix27-293
β-strand3214
Chains H and L: 1 helix, 1 β-strand
ElementResiduesLengthSheet
α-helix27-293
β-strand32-3328
Chain K: 2 helices, 1 β-strand
ElementResiduesLengthSheet
α-helix271
β-strand28115
α-helix301

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Peptidyl-prolyl cis-trans isomerase SlyDA, B, C, Dprotein153Thermus thermophilusQ5SLE7 (AlphaFold model)
30S ribosomal protein S2E, F, G, H, I, J, K, L, Mprotein16Escherichia coliP0A7V0 (AlphaFold model)
Sequence of entity 1 (A, B, C, D), FASTA
>4ODM_1 Peptidyl-prolyl cis-trans isomerase SlyD (chains A, B, C, D)
MKVGQDKVVTIRYTLQVEGEVLDQGELSYLHGHRNLIPGLEEALEGREEGEAFQAHVPAE
KAYGPHDPEGVQVVPLSAFPEDAEVVPGAQFYAQDMEGNPMPLTVVAVEGEEVTVDFNHP
LAGKDLDFQVEVVKVREATPEELLHGHAHLVPK
Sequence of entity 2 (E, F, G, H, I, J, K, L, M), FASTA
>4ODM_2 30S ribosomal protein S2 (chains E, F, G, H, I, J, K, L, M)
TRYANPKMKPFIFGAX

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:

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