Research workbench
The closed state of RGLG1 vwa domain with midas is occupied by water
Analyse The closed state of RGLG1 vwa domain with midas is occupied by water in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6K87
- Type
- protein
- Length
- 282 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- E3 ubiquitin-protein ligase RGLG1
- EC
- 2.3.2.27
- UniProt
- Q9SS90
- Pockets
- 3 · best druggability 0.46
Structure
x-ray diffraction · 1 distinct chain · 40% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B | E3 ubiquitin-protein ligase RGLG1 (EC 2.3.2.27) | protein | 282 | 40% helix, 15% strand | Q9SS90 |
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 126 | 0.46 | 0.78 | 18 | empty |
| 2 | 88 | 0.34 | 0.74 | 19 | empty |
| 3 | 59 | 0.29 | 0.74 | 16 | empty |
Compared structures
- 6K87 · The closed state of RGLG1 VWA domain with MIDAS is occupied by water · the same entry in another collection · chain B against B, TM-score 1.00
- Q9SS90 · AlphaFold monomer V2.0 prediction for E3 ubiquitin-protein ligase RGLG1 (Q9SS90) · a predicted model of the same protein · chain B against A, TM-score 0.93
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 Q9SS90
- Elsewhere: RCSB PDB 6K87 · PDBe 6K87 · UniProt Q9SS90
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