Research workbench
AlphaFold monomer V2.0 prediction for protein transport protein SEC13 (P53024)
Analyse AlphaFold monomer V2.0 prediction for protein transport protein SEC13 (P53024) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P53024
- Type
- protein
- Length
- 289 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x0802a4d42FE33Ea91364Adff0d1651923952Ab99
- Molecule
- Protein transport protein SEC13
- UniProt
- P53024
- Pockets
- 3 · best druggability 0.73
Structure
1 distinct chain · 2% helix, 56% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein transport protein SEC13 | protein | 289 | 2% helix, 56% strand | P53024 |
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 810 | 0.73 | 0.78 | 55 | empty |
| 2 | 107 | 0.44 | 0.79 | 22 | empty |
| 3 | 74 | 0.38 | 0.77 | 14 | empty |
Compared structures
- 4L9O · Crystal Structure of the Sec13-Sec16 blade-inserted complex from Pichia pastoris · an experimental structure of the same protein · chain A against B, TM-score 0.96
- 4L9O · Crystal structure of the SEC13-SEC16 blade-inserted complex from pichia pastoris · an experimental structure of the same protein · chain A against B, TM-score 0.96
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 P53024
- Elsewhere: UniProt P53024 · AlphaFold DB P53024
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