MolNFT v1 · #17321 · protein
Crystal structure of the traffic ATPase (HP0525) of the helicobacter pylori type IV secretion system bound by sulfate
1OPX · VIRB11 homolog: “Crystal structure of the traffic ATPase (HP0525) of the helicobacter pylori type IV secretion system bound by…”. X-ray diffraction, 1 ligand (SO4), 6 pockets (best druggability 0.82). MolNFT v1 #17321 on GenesisL1…
- PDB
- 1OPX
- Type
- protein
- Length
- 646 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- VIRB11 homolog
- UniProt
- Q7BK04
- Ligands
- SO4
- Pockets
- 6 · best druggability 0.82
Structure
x-ray diffraction · 1 distinct chain · 39% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | VIRB11 homolog | protein | 323 | 39% helix, 22% strand | Q7BK04 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1120 | 0.82 | 0.83 | 89 | SO4 |
| 2 | 1164 | 0.76 | 0.78 | 95 | SO4 |
| 3 | 83 | 0.38 | 0.77 | 21 | empty |
| 4 | 121 | 0.38 | 0.74 | 23 | empty |
| 5 | 64 | 0.35 | 0.77 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 1879 Ų buried · 20 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 12 modified (engineered).
Compared structures
- 1OPX · Crystal structure of the traffic ATPase (HP0525) of the Helicobacter pylori type IV… · the same entry in another collection · 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 Q7BK04
- Elsewhere: RCSB PDB 1OPX · PDBe 1OPX · UniProt Q7BK04
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