Research workbench
AlphaFold monomer V2.0 prediction for origin recognition complex subunit 5 (Q54C22)
Analyse AlphaFold monomer V2.0 prediction for origin recognition complex subunit 5… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q54C22
- Type
- protein
- Length
- 571 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xea70C1c161ad1752A036904c1B96f7dCc33d1aFb
- Molecule
- Origin recognition complex subunit 5
- UniProt
- Q54C22
- Pockets
- 6 · best druggability 0.65
Structure
1 distinct chain · 46% helix, 7% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Origin recognition complex subunit 5 | protein | 571 | 46% helix, 7% strand | Q54C22 |
Pockets
6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 590 | 0.65 | 0.76 | 52 | empty |
| 2 | 340 | 0.54 | 0.74 | 34 | empty |
| 3 | 176 | 0.51 | 0.78 | 19 | empty |
| 4 | 187 | 0.48 | 0.76 | 27 | empty |
| 5 | 126 | 0.39 | 0.74 | 17 | 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 Q54C22
- Elsewhere: UniProt Q54C22 · AlphaFold DB Q54C22
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