Research workbench
AlphaFold monomer V2.0 prediction for origin recognition complex subunit 1 (Q54RM2)
Analyse AlphaFold monomer V2.0 prediction for origin recognition complex subunit 1… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q54RM2
- Type
- protein
- Length
- 631 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x5AF1007bEEe0CF438B019cDFeDD7CfAd3AB7afA8
- Molecule
- Origin recognition complex subunit 1
- UniProt
- Q54RM2
- Pockets
- 4 · best druggability 0.65
Structure
1 distinct chain · 39% helix, 7% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Origin recognition complex subunit 1 | protein | 631 | 39% helix, 7% strand | Q54RM2 |
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 201 | 0.65 | 0.84 | 29 | empty |
| 2 | 119 | 0.39 | 0.74 | 23 | empty |
| 3 | 66 | 0.36 | 0.78 | 12 | empty |
| 4 | 73 | 0.35 | 0.76 | 11 | 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 Q54RM2
- Elsewhere: UniProt Q54RM2 · AlphaFold DB Q54RM2
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