Research workbench
Reduced hlyu from vibrio cholerae N16961
Analyse Reduced hlyu from vibrio cholerae N16961 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4OOI
- Type
- protein
- Length
- 377 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Transcriptional activator hlyu
- UniProt
- P52695
- Pockets
- 1 · best druggability 0.54
Structure
x-ray diffraction · 4 distinct chains · 62% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Transcriptional activator hlyu | protein | 95 | 62% helix, 15% strand | P52695 |
| B | Transcriptional activator hlyu | protein | 96 | 64% helix, 15% strand | P52695 |
| C | Transcriptional activator hlyu | protein | 94 | 63% helix, 13% strand | P52695 |
| D | Transcriptional activator hlyu | protein | 92 | 60% helix, 13% strand | P52695 |
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 256 | 0.54 | 0.77 | 33 | empty |
Interfaces
3 interfaces between chains.
- A–B · 1491 Ų buried · 2 hydrogen bonds · protein-protein
- C–D · 1417 Ų buried · 3 hydrogen bonds · protein-protein
- B–D · 103 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
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 P52695
- Elsewhere: RCSB PDB 4OOI · PDBe 4OOI · UniProt P52695
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.