Research workbench
Putative thiosulfate sulfurtransferase ynje
Analyse Putative thiosulfate sulfurtransferase ynje in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2WLR
- Type
- protein
- Length
- 408 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Putative thiosulfate sulfurtransferase ynje
- EC
- 2.8.1.1
- UniProt
- P78067
- Pockets
- 5 · best druggability 0.53
Structure
x-ray diffraction · 1 distinct chain · 33% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Putative thiosulfate sulfurtransferase ynje (EC 2.8.1.1) | protein | 408 | 33% helix, 17% strand | P78067 |
Ligands and binding sites
- EPE · 4-(2-hydroxyethyl)-1-piperazine ethanesulfonic acid · additive · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 228 | 0.53 | 0.77 | 29 | empty |
| 2 | 147 | 0.48 | 0.77 | 18 | empty |
| 3 | 80 | 0.35 | 0.75 | 14 | EPE |
| 4 | 89 | 0.34 | 0.74 | 19 | empty |
| 5 | 51 | 0.32 | 0.77 | 15 | empty |
Modifications
Observed in the structure: 11 modified (engineered, oxidation).
Compared structures
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 P78067
- Elsewhere: RCSB PDB 2WLR · PDBe 2WLR · UniProt P78067
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