Research workbench
Structure of the glycoside hydrolase domain of pela variant E218A from pseudomonas aeruginosa
Analyse Structure of the glycoside hydrolase domain of pela variant E218A from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5TSY
- Type
- protein
- Length
- 253 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Pela
- UniProt
- Q9HZE4
- Pockets
- 2 · best druggability 0.55
Structure
x-ray diffraction · 1 distinct chain · 40% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Pela | protein | 253 | 40% helix, 23% strand | Q9HZE4 |
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 | 328 | 0.55 | 0.75 | 39 | empty |
| 2 | 76 | 0.36 | 0.76 | 11 | empty |
Compared structures
- 5TSY · Structure of the glycoside hydrolase domain of PelA variant E218A 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 Q9HZE4
- Elsewhere: RCSB PDB 5TSY · PDBe 5TSY · UniProt Q9HZE4
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