Research workbench
Structure of membrane binding protein pleurotolysin a from pleurotus ostreatus
Analyse Structure of membrane binding protein pleurotolysin a from pleurotus ostreatus in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4OEB
- Type
- protein
- Length
- 540 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Pleurotolysin a
- UniProt
- Q8X1M9
- Ligands
- SO4
- Pockets
- 4 · best druggability 0.84
Structure
x-ray diffraction · 1 distinct chain · 2% helix, 59% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Pleurotolysin a | protein | 135 | 2% helix, 59% strand | Q8X1M9 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 940 | 0.84 | 0.86 | 119 | empty |
| 2 | 114 | 0.35 | 0.73 | 27 | empty |
| 3 | 65 | 0.34 | 0.77 | 17 | empty |
| 4 | 50 | 0.28 | 0.75 | 16 | empty |
Interfaces
5 interfaces between chains.
- A–D · 564 Ų buried · 10 hydrogen bonds · protein-protein
- A–B · 555 Ų buried · 12 hydrogen bonds · protein-protein
- B–C · 531 Ų buried · 9 hydrogen bonds · protein-protein
- B–D · 236 Ų buried · 3 hydrogen bonds · protein-protein
- A–C · 231 Ų buried · 3 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 modified (engineered).
Compared structures
- 4OEB · Structure of membrane binding protein pleurotolysin A from Pleurotus ostreatus · 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 Q8X1M9
- Elsewhere: RCSB PDB 4OEB · PDBe 4OEB · UniProt Q8X1M9
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