MolNFT v1 · #111602 · protein
X-ray structure of helicobacter pylori cagl-K74
4YVM · Cag pathogenicity island protein: “X-ray structure of helicobacter pylori cagl-K74”. X-ray diffraction, 5 pockets (best druggability 0.60). MolNFT v1 #111602 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 4YVM
- Type
- protein
- Length
- 406 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cag pathogenicity island protein
- UniProt
- Q75XL3
- Pockets
- 5 · best druggability 0.60
Structure
x-ray diffraction · 2 distinct chains · 83% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cag pathogenicity island protein | protein | 202 | 83% helix, 0% strand | Q75XL3 |
| B | Cag pathogenicity island protein | protein | 204 | 83% helix, 0% strand | Q75XL3 |
Pockets
5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 469 | 0.60 | 0.74 | 36 | empty |
| 2 | 419 | 0.57 | 0.74 | 34 | empty |
| 3 | 66 | 0.50 | 0.84 | 16 | empty |
| 4 | 68 | 0.34 | 0.76 | 15 | empty |
| 5 | 50 | 0.24 | 0.72 | 11 | empty |
Interfaces
1 interface between chains.
- A–B · 1778 Ų buried · 23 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 4YVM · X-ray structure of Helicobacter pylori CagL-K74 · the same entry in another collection · chain B against B, 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 Q75XL3
- Elsewhere: RCSB PDB 4YVM · PDBe 4YVM · UniProt Q75XL3
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.