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Solution structure of peptidyl-prolyl cis-trans isomerase from burkholderia pseudomallei complexed with cycloheximide-N- ethylethanoate
Analyse Solution structure of peptidyl-prolyl cis-trans isomerase from burkholderia… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2KO7
- Type
- protein
- Length
- 117 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Peptidyl-prolyl cis-trans isomerase
- EC
- 5.2.1.8
- UniProt
- Q63J95
- Ligands
- JZF
Structure
solution nmr · 1 distinct chain · 11% helix, 37% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Peptidyl-prolyl cis-trans isomerase (EC 5.2.1.8) | protein | 117 | 11% helix, 37% strand | Q63J95 |
Ligands and binding sites
- JZF · ethyl (4-{(2R)-2-[(1S,3S,5S)-3,5-dimethyl-2-oxocyclohexyl]-2-hydroxyethyl}-2,6-dioxopiperidin-1-yl)acetate · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 2KO7 · Solution structure of peptidyl-prolyl cis-trans isomerase from Burkholderia pseudomallei… · the same entry in another collection · chain A against A, TM-score 1.00
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt Q63J95
- Elsewhere: RCSB PDB 2KO7 · PDBe 2KO7 · UniProt Q63J95
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