Research workbench
Crystal structure of helicobacter pylori uree bound to NI2+
Analyse Crystal structure of helicobacter pylori uree bound to NI2+ in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3TJ8
- Type
- protein
- Length
- 301 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Urease accessory protein uree
- UniProt
- Q09064
- Ligands
- NI
Structure
x-ray diffraction · 2 distinct chains · 23% helix, 38% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Urease accessory protein uree | protein | 149 | 24% helix, 39% strand | Q09064 |
| B | Urease accessory protein uree | protein | 152 | 22% helix, 36% strand | Q09064 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–B · 1274 Ų buried · 25 hydrogen bonds · protein-protein
Compared structures
- 3TJ8 · Crystal structure of Helicobacter pylori UreE bound to Ni2+ · the same entry in another collection · chain A against A, TM-score 1.00
- Q09064 · AlphaFold monomer V2.0 prediction for urease accessory protein uree (Q09064) · a predicted model of the same protein · chain A 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 Q09064
- Elsewhere: RCSB PDB 3TJ8 · PDBe 3TJ8 · UniProt Q09064
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.