Research workbench
Pore-forming thermostable direct hemolysin from grimontia hollisae
Analyse Pore-forming thermostable direct hemolysin from grimontia hollisae in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4WX5
- Type
- protein
- Length
- 616 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hemolysin, heat labile
- UniProt
- P14711
- Pockets
- 8 · best druggability 0.61
Structure
x-ray diffraction · 1 distinct chain · 10% helix, 56% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Hemolysin, heat labile | protein | 154 | 10% helix, 56% strand | P14711 |
Pockets
8 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 380 | 0.61 | 0.77 | 60 | empty |
| 2 | 374 | 0.59 | 0.76 | 42 | empty |
| 3 | 196 | 0.54 | 0.79 | 42 | empty |
| 4 | 169 | 0.48 | 0.77 | 35 | empty |
| 5 | 91 | 0.45 | 0.80 | 19 | empty |
Interfaces
4 interfaces between chains.
- A–D · 675 Ų buried · 12 hydrogen bonds · protein-protein
- A–C · 489 Ų buried · 2 hydrogen bonds · protein-protein
- B–D · 484 Ų buried · 3 hydrogen bonds · protein-protein
- B–C · 56 Ų buried · 1 hydrogen bond · protein-protein
Modifications
Observed in the structure: 4 disulfide (disulfide).
Compared structures
- 4WX5 · pore-forming thermostable direct hemolysin from Grimontia hollisae · the same entry in another collection · chain A against A, TM-score 1.00
- P14711 · AlphaFold monomer V2.0 prediction for hemolysin, heat labile (P14711) · a predicted model of the same protein · 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 P14711
- Elsewhere: RCSB PDB 4WX5 · PDBe 4WX5 · UniProt P14711
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