Research workbench
AlphaFold monomer V2.0 prediction for er membrane protein complex subunit 1 (Q5R7K6)
Analyse AlphaFold monomer V2.0 prediction for er membrane protein 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
- Q5R7K6
- Type
- protein
- Length
- 996 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x7782F4817b37743d738e9aF842bf74bd50f2015E
- Molecule
- Er membrane protein complex subunit 1
- UniProt
- Q5R7K6
- Pockets
- 11 · best druggability 0.76
Structure
1 distinct chain · 13% helix, 43% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Er membrane protein complex subunit 1 | protein | 996 | 13% helix, 43% strand | Q5R7K6 |
Pockets
11 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 962 | 0.76 | 0.78 | 54 | empty |
| 2 | 897 | 0.74 | 0.78 | 81 | empty |
| 3 | 375 | 0.65 | 0.79 | 30 | empty |
| 4 | 228 | 0.57 | 0.79 | 23 | empty |
| 5 | 61 | 0.56 | 0.89 | 17 | empty |
Modifications
Observed in the structure: 2 disulfide (disulfide).
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 Q5R7K6
- Elsewhere: UniProt Q5R7K6 · AlphaFold DB Q5R7K6
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