Research workbench
1.6 a crystal structure of peptidyl-prolyl cis-trans isomerase ppiase from pseudomonas syringae pv. tomato str. DC3000 (pspto DC3000)
Analyse 1.6 a crystal structure of peptidyl-prolyl cis-trans isomerase ppiase from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5XB0
- Type
- protein
- Length
- 133 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Peptidyl-prolyl cis-trans isomerase
- EC
- 5.2.1.8
- UniProt
- Q88B84
- Pockets
- 2 · best druggability 0.37
Structure
x-ray diffraction · 1 distinct chain · 26% helix, 33% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Peptidyl-prolyl cis-trans isomerase (EC 5.2.1.8) | protein | 133 | 26% helix, 33% strand | Q88B84 |
Ligands and binding sites
- TLA · L(+)-tartaric acid · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 54 | 0.37 | 0.79 | 10 | TLA |
| 2 | 56 | 0.27 | 0.73 | 17 | empty |
Compared structures
- 5XB0 · 1.6 A crystal structure of peptidyl-prolyl cis-trans isomerase PPIase from Pseudomonas… · 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 Q88B84
- Elsewhere: RCSB PDB 5XB0 · PDBe 5XB0 · UniProt Q88B84
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.