Research workbench
Opua inhibited inward facing
Analyse Opua inhibited inward facing in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7AHE
- Type
- protein
- Length
- 1,308 residues
- Chains
- 4
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- ABC transporter permease subunit; ABC-type PROLINE/GLYCINE betaine transport system…
- UniProt
- A0A0V8ETW8, A0A0R2NIU5
- Ligands
- 2BA
- Pockets
- 19 · best druggability 0.79
Structure
electron microscopy · 2 distinct chains · 56% helix, 9% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | ABC transporter permease subunit | protein | 272 | 83% helix, 0% strand | A0A0V8ETW8 |
| C, D | ABC-type PROLINE/GLYCINE betaine transport system ATPase component | protein | 382 | 37% helix, 16% strand | A0A0R2NIU5 |
Ligands and binding sites
- 2BA · (2r,3r,3as,5r,7ar,9r,10r,10as,12r,14ar)-2,9-bis(6-amino-9H-purin-9-yl)octahydro-2H,7H-difuro[3,2-D:3', 2'-J][1,3,7,9,2,8 ]tetraoxadiphosphacyclododecine-3,5, 10,12-tetrol 5,12-dioxide · ligand · chains C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
19 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1041 | 0.79 | 0.81 | 90 | 2BA |
| 2 | 684 | 0.75 | 0.81 | 65 | empty |
| 3 | 193 | 0.61 | 0.82 | 26 | empty |
| 4 | 219 | 0.58 | 0.79 | 27 | empty |
| 5 | 249 | 0.58 | 0.78 | 29 | empty |
Interfaces
4 interfaces between chains.
- C–D · 2195 Ų buried · 7 hydrogen bonds · protein-protein
- A–B · 1874 Ų buried · 12 hydrogen bonds · protein-protein
- B–D · 894 Ų buried · 11 hydrogen bonds · protein-protein
- A–C · 868 Ų buried · 9 hydrogen bonds · protein-protein
Compared structures
- 7AHE · OpuA inhibited inward facing · 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 A0A0V8ETW8
- Every structure of UniProt A0A0R2NIU5
- Elsewhere: RCSB PDB 7AHE · PDBe 7AHE · UniProt A0A0V8ETW8 · UniProt A0A0R2NIU5
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