Research workbench
AlphaFold monomer V2.0 prediction for origin recognition complex subunit 2 (Q91628)
Analyse AlphaFold monomer V2.0 prediction for origin recognition complex subunit 2… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q91628
- Type
- protein
- Length
- 558 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xb4D2d9c96b0D792d0b77e7147D724cc1F801ae58
- Molecule
- Origin recognition complex subunit 2
- UniProt
- Q91628
- Pockets
- 7 · best druggability 0.59
Structure
1 distinct chain · 35% helix, 7% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Origin recognition complex subunit 2 | protein | 558 | 35% helix, 7% strand | Q91628 |
Pockets
7 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 212 | 0.59 | 0.81 | 24 | empty |
| 2 | 219 | 0.57 | 0.79 | 24 | empty |
| 3 | 179 | 0.49 | 0.76 | 21 | empty |
| 4 | 145 | 0.41 | 0.74 | 22 | empty |
| 5 | 89 | 0.40 | 0.77 | 19 | empty |
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 Q91628
- Elsewhere: UniProt Q91628 · AlphaFold DB Q91628
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