7OXJ: TtSlyD with M8A pseudo-wild-type S2 peptide

ttSlyD with M8A pseudo-wild-type S2 peptide. Determined by X-ray diffraction at 1.85 Å resolution. Released 16 Mar 2022.

Method
X-ray diffraction
Resolution
1.85 Å
Organisms
Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8), Escherichia coli (strain K12), synthetic construct
Chains
3
Atoms
1,389
Mol. weight
19.92 kDa
Ligands
NI, MG
Released
16 Mar 2022

Explore 7OXJ in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

7OXJ contains 7 α-helices and 13 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: 7 helices, 12 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-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
β-strand153-15532
Chain D: 0 helices, 1 β-strand
ElementResiduesLengthSheet
β-strand913

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Peptidyl-prolyl cis-trans isomeraseAprotein158Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8)Q5SLE7 (AlphaFold model)
30S ribosomal protein S2Dprotein15Escherichia coli (strain K12)P0A7V0 (AlphaFold model)
Fragment of 30S ribosomal protein S2 peptideEprotein2synthetic construct
Sequence of entity 1 (A), FASTA
>7OXJ_1 Peptidyl-prolyl cis-trans isomerase (chains A)
MKVGQDKVVTIRYTLQVEGEVLDQGELSYLHGHRNLIPGLEEALEGREEGEAFQAHVPAE
KAYGPHDPEGVQVVPLSAFPEDAEVVPGAQFYAQDMEGNPMPLTVVAVEGEEVTVDFNHP
LAGKDLDFQVEVVKVREATPEELLHGHAHPSGHHHHHH
Sequence of entity 2 (D), FASTA
>7OXJ_2 30S ribosomal protein S2 (chains D)
TRYWNAKALPFAFGA
Sequence of entity 3 (E), FASTA
>7OXJ_3 Fragment of 30S ribosomal protein S2 peptide (chains E)
XX

Ligands and cofactors

IDNameFormulaCopies
NINickel (II) ionNi1
MGMagnesium ionMg1

Water and common crystallization additives (PGE, PG4, CL) are not listed.

Primary citation

Impact of distant peptide substrate residues on enzymatic activity of SlyD. Pazicky, S., Werle, A.A., Lei, J. et al. Cell Mol Life Sci (2022) 79:138-138. DOI 10.1007/s00018-022-04179-4 · 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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