Research workbench
NMR structure of the putative GTPase-activating (gap) domain of vope
Analyse NMR structure of the putative GTPase-activating (gap) domain of vope in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6X6N
- Type
- protein
- Length
- 134 residues
- Chains
- 1
- Method
- solution nmr; solution scattering
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Outer membrane virulence protein yope
- UniProt
- A0A655XAV0
- Pockets
- 2 · best druggability 0.69
Structure
solution nmr; solution scattering · 1 distinct chain · 60% helix, 3% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Outer membrane virulence protein yope | protein | 134 | 60% helix, 3% strand | A0A655XAV0 |
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 336 | 0.69 | 0.82 | 45 | empty |
| 2 | 330 | 0.66 | 0.80 | 45 | empty |
Compared structures
- 6X6N · NMR structure of the putative GTPase-Activating (GAP) domain of VopE · 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 A0A655XAV0
- Elsewhere: RCSB PDB 6X6N · PDBe 6X6N · UniProt A0A655XAV0
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