Research workbench
Native crystal structure of helicobacter pylori urease accessory protein uref
Analyse Native crystal structure of helicobacter pylori urease accessory protein uref in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3O1Q
- Type
- protein
- Length
- 623 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Urease accessory protein uref
- UniProt
- Q09065
- Pockets
- 4 · best druggability 0.75
Structure
x-ray diffraction · 2 distinct chains · 73% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | Urease accessory protein uref | protein | 210 | 73% helix, 0% strand | Q09065 |
| B | Urease accessory protein uref | protein | 203 | 73% helix, 0% strand | Q09065 |
Pockets
4 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 543 | 0.75 | 0.83 | 51 | empty |
| 2 | 638 | 0.73 | 0.79 | 63 | empty |
| 3 | 176 | 0.69 | 0.88 | 31 | empty |
| 4 | 229 | 0.56 | 0.79 | 30 | empty |
Interfaces
3 interfaces between chains.
- B–C · 1736 Ų buried · 22 hydrogen bonds · protein-protein
- A–B · 459 Ų buried · 3 hydrogen bonds · protein-protein
- A–C · 291 Ų buried · 2 hydrogen bonds · protein-protein
Compared structures
- 3O1Q · Native Crystal Structure of Helicobacter pylori Urease Accessory Protein UreF · the same entry in another collection · chain A against A, TM-score 1.00
- Q09065 · AlphaFold monomer V2.0 prediction for urease accessory protein uref (Q09065) · a predicted model of the same protein · chain B against A, TM-score 0.99
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 Q09065
- Elsewhere: RCSB PDB 3O1Q · PDBe 3O1Q · UniProt Q09065
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.