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
| 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 | 38-44 | 7 | |
| α-helix | 47 | 1 | |
| β-strand | 48 | 1 | 1 |
| β-strand | 52-57 | 6 | 2 |
| α-helix | 59-61 | 3 | |
| α-helix | 65-67 | 3 | |
| α-helix | 68-70 | 3 | |
| β-strand | 71-75 | 5 | 4 |
| α-helix | 76-78 | 3 | |
| β-strand | 90-94 | 5 | 4 |
| β-strand | 100-109 | 10 | 4 |
| β-strand | 112-116 | 5 | 4 |
| β-strand | 126-137 | 12 | 2 |
| α-helix | 138-139 | 2 | |
| α-helix | 140-145 | 6 | |
Chain C: 9 helices, 11 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 2 | 1 | 9 |
| β-strand | 7-17 | 11 | 10 |
| β-strand | 20-30 | 11 | 10 |
| β-strand | 36 | 1 | 11 |
| α-helix | 38-44 | 7 | |
| α-helix | 47 | 1 | |
| β-strand | 48 | 1 | 9 |
| β-strand | 52-57 | 6 | 10 |
| α-helix | 59-61 | 3 | |
| α-helix | 65-67 | 3 | |
| α-helix | 68-70 | 3 | |
| β-strand | 71-75 | 5 | 12 |
| α-helix | 76-78 | 3 | |
| β-strand | 90-94 | 5 | 12 |
| β-strand | 100-109 | 10 | 12 |
| β-strand | 112-116 | 5 | 12 |
| β-strand | 126-137 | 12 | 10 |
| α-helix | 138-139 | 2 | |
| α-helix | 140-145 | 6 | |
| α-helix | 148-150 | 3 | |
Chain D: 9 helices, 11 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 2 | 1 | 13 |
| β-strand | 7-17 | 11 | 14 |
| β-strand | 20-30 | 11 | 14 |
| β-strand | 36 | 1 | 15 |
| α-helix | 38-44 | 7 | |
| α-helix | 47 | 1 | |
| β-strand | 48 | 1 | 13 |
| β-strand | 52-57 | 6 | 14 |
| α-helix | 59-61 | 3 | |
| α-helix | 65-67 | 3 | |
| α-helix | 68-70 | 3 | |
| β-strand | 71-75 | 5 | 16 |
| α-helix | 76-78 | 3 | |
| α-helix | 80 | 1 | |
| β-strand | 90-94 | 5 | 16 |
| β-strand | 100-109 | 10 | 16 |
| β-strand | 112-116 | 5 | 16 |
| β-strand | 126-137 | 12 | 14 |
| α-helix | 138-139 | 2 | |
| α-helix | 140-145 | 6 | |
Chains E, G and I: 0 helices, 1 β-strand
| Element | Residues | Length | Sheet |
|---|
| β-strand | 28 | 1 | 3 |
Chains F and J: 1 helix, 1 β-strand
| Element | Residues | Length | Sheet |
|---|
| α-helix | 27-29 | 3 | |
| β-strand | 32 | 1 | 4 |
Chains H and L: 1 helix, 1 β-strand
| Element | Residues | Length | Sheet |
|---|
| α-helix | 27-29 | 3 | |
| β-strand | 32-33 | 2 | 8 |
Chain K: 2 helices, 1 β-strand
| Element | Residues | Length | Sheet |
|---|
| α-helix | 27 | 1 | |
| β-strand | 28 | 1 | 15 |
| α-helix | 30 | 1 | |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Peptidyl-prolyl cis-trans isomerase SlyD | A, B, C, D | protein | 153 | Thermus thermophilus | Q5SLE7 (AlphaFold model) |
| 30S ribosomal protein S2 | E, F, G, H, I, J, K, L, M | protein | 16 | Escherichia coli | P0A7V0 (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:
- 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
- 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
- 7OXG 2.0 Å, ttSlyD FKBP domain with M8A pseudo-wild-type S2 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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