Research workbench
Crystal structure of protein of unknown function PA2260 from pseudomonas aeruginosa, possible sugar phosphate isomerase
Analyse Crystal structure of protein of unknown function PA2260 from pseudomonas… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1YX1
- Type
- protein
- Length
- 751 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hypothetical protein PA2260
- UniProt
- Q9I1L3
- Ligands
- NA
- Pockets
- 7 · best druggability 0.83
Structure
x-ray diffraction · 2 distinct chains · 43% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | Hypothetical protein PA2260 | protein | 250 | 44% helix, 23% strand | Q9I1L3 |
| B | Hypothetical protein PA2260 | protein | 251 | 42% helix, 22% strand | Q9I1L3 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 522 | 0.83 | 0.89 | 70 | empty |
| 2 | 65 | 0.61 | 0.91 | 18 | empty |
| 3 | 65 | 0.53 | 0.87 | 20 | empty |
| 4 | 150 | 0.40 | 0.74 | 22 | NA |
| 5 | 139 | 0.40 | 0.74 | 25 | empty |
Interfaces
3 interfaces between chains.
- A–B · 812 Ų buried · 12 hydrogen bonds · protein-protein
- B–C · 792 Ų buried · 11 hydrogen bonds · protein-protein
- A–C · 755 Ų buried · 11 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 modified (engineered).
Compared structures
- 1YX1 · Crystal Structure of Protein of Unknown Function PA2260 from Pseudomonas aeruginosa… · 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 Q9I1L3
- Elsewhere: RCSB PDB 1YX1 · PDBe 1YX1 · UniProt Q9I1L3
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