7OXG: PDB entry 7OXG

ttSlyD FKBP domain with M8A pseudo-wild-type S2 peptide. Determined by X-ray diffraction at 2.0 Å resolution. Released 16 Mar 2022.

Method: X-ray diffraction
Resolution: 2.0 Å
Organisms: Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8), Escherichia coli (strain K12)
Chains: 4
Atoms: 1,849
Mol. weight: 27.93 kDa
Released: 16 Mar 2022

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

Secondary structure: helices and β-sheets

7OXG contains 13 α-helices and 14 β-strands across 4 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: 6 helices, 7 β-strands

Element	Residues	Length	Sheet
β-strand	2	1	1
β-strand	7-17	11	2
β-strand	20-30	11	2
β-strand	36	1	3
α-helix	40-44	5
α-helix	47	1
β-strand	48	1	1
β-strand	52-58	7	2
α-helix	59-61	3
α-helix	73	1
β-strand	77-89	13	2
α-helix	90-91	2
α-helix	92-97	6

Chain B: 4 helices, 6 β-strands

Element	Residues	Length	Sheet
β-strand	2	1	4
β-strand	7-17	11	5
β-strand	20-30	11	5
α-helix	40-44	5
α-helix	47	1
β-strand	48	1	4
β-strand	52-58	7	5
β-strand	77-89	13	5
α-helix	90-91	2
α-helix	92-97	6

Chain C: 2 helices, 1 β-strand

Element	Residues	Length	Sheet
α-helix	4-6	3
β-strand	11	1	3
α-helix	12-13	2

Chain D: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	4-6	3

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Peptidyl-prolyl cis-trans isomerase,Peptidyl-prolyl cis-trans isomerase	A, B	protein	110	Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8)	Q5SLE7 (AlphaFold model)
30S ribosomal protein S2	C, D	protein	15	Escherichia coli (strain K12)	P0A7V0 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>7OXG_1 Peptidyl-prolyl cis-trans isomerase,Peptidyl-prolyl cis-trans isomerase (chains A, B)
MKVGQDKVVTIRYTLQVEGEVLDQGELSYLHGHRNLIPGLEEALEGREEGEAFQAHVPAE
KAYGATGHPGIIPPHATLDFQVEVVKVREATPEELLHGHAHPSGHHHHHH

Sequence of entity 2 (C, D), FASTA

>7OXG_2 30S ribosomal protein S2 (chains C, D)
TRYWNAKALPFAFGA

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:

4ODK 1.4 Å, Structure of SlyD from Thermus thermophilus in complex with T1 peptide
4ODN 1.6 Å, Structure of SlyD from Thermus thermophilus in complex with S2-plus peptide
4ODO 1.6 Å, Structure of SlyD from Thermus thermophilus in complex with FK506
7OXH 1.7 Å, ttSlyD with pseudo-wild-type S2 peptide
4ODP 1.75 Å, Structure of SlyD delta-IF from Thermus thermophilus in complex with S2-W23A peptide
4ODM 1.75 Å, Structure of SlyD from Thermus thermophilus in complex with S2-W23A peptide
7OXJ 1.85 Å, ttSlyD with M8A pseudo-wild-type S2 peptide
4ODR 1.93 Å, Structure of SlyD delta-IF from Thermus thermophilus in complex with FK506
4ODQ 2.0 Å, Structure of SlyD delta-IF from Thermus thermophilus in complex with S3 peptide
3CGM 2.41 Å, Crystal structure of thermophilic SlyD
3LUO 2.55 Å, Crystal Structure and functional characterization of the thermophilic prolyl isomerase…
7OXI 2.6 Å, ttSlyD with W4A pseudo-wild-type S2 peptide

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