Research workbench
Crystal structure of a smt fusion peptidyl-prolyl cis-trans isomerase with a G95A surface mutation from burkholderia pseudomallei complexed with FK506
Analyse Crystal structure of a smt fusion peptidyl-prolyl cis-trans isomerase with a… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3UF8
- Type
- protein
- Length
- 192 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ubiquitin-like protein SMT3, peptidyl-prolyl cis-trans isomerase
- EC
- 5.2.1.8
- UniProt
- Q12306, Q3JK38
- Ligands
- FK5
- Pockets
- 2 · best druggability 0.55
Structure
x-ray diffraction · 1 distinct chain · 14% helix, 37% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ubiquitin-like protein SMT3, peptidyl-prolyl cis-trans isomerase (EC 5.2.1.8) | protein | 192 | 14% helix, 37% strand | Q12306, Q3JK38 |
Ligands and binding sites
- FK5 · 8-deethyl-8-[but-3-enyl]-ascomycin · ligand · 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, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 262 | 0.55 | 0.77 | 32 | empty |
| 2 | 65 | 0.37 | 0.77 | 13 | empty |
Compared structures
- 3UF8 · Crystal structure of a SMT fusion Peptidyl-prolyl cis-trans isomerase with a G95A surface… · the same entry in another collection · chain A against A, TM-score 1.00
- Q12306 · AlphaFold monomer V2.0 prediction for ubiquitin-like protein SMT3 (Q12306) · a predicted model of the same protein · chain A against A, TM-score 0.40
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 Q12306
- Every structure of UniProt Q3JK38
- Elsewhere: RCSB PDB 3UF8 · PDBe 3UF8 · UniProt Q12306 · UniProt Q3JK38
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