Research workbench
Crystal structure of a PSPTO_0244 (protein with unknown function which belongs to pfam DUF861 family) from pseudomonas syringae pv. tomato str. DC3000 at 1.30 a resolution
Analyse Crystal structure of a PSPTO_0244 (protein with unknown function which belongs… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3MYX
- Type
- protein
- Length
- 470 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Uncharacterized protein PSPTO_0244
- UniProt
- Q88AY9
- Ligands
- CL
- Pockets
- 4 · best druggability 0.62
Structure
x-ray diffraction · 1 distinct chain · 1% helix, 52% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Uncharacterized protein PSPTO_0244 | protein | 235 | 1% helix, 52% strand | Q88AY9 |
Ligands and binding sites
- CL · Chloride ion · ion · 2 copies · chains A, B
- EDO · 1,2-ethanediol · additive · 11 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 288 | 0.62 | 0.79 | 26 | EDO |
| 2 | 281 | 0.60 | 0.79 | 24 | EDO |
| 3 | 97 | 0.42 | 0.78 | 20 | empty |
| 4 | 110 | 0.39 | 0.76 | 24 | empty |
Interfaces
1 interface between chains.
- A–B · 369 Ų buried · 6 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 8 modified (engineered).
Compared structures
- 3MYX · Crystal structure of a PSPTO_0244 (Protein with unknown function which belongs to Pfam… · 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 Q88AY9
- Elsewhere: RCSB PDB 3MYX · PDBe 3MYX · UniProt Q88AY9
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