Research workbench
AlphaFold monomer V2.0 prediction for pro-pro endopeptidase (K4ZRC1)
Analyse AlphaFold monomer V2.0 prediction for pro-pro endopeptidase (K4ZRC1) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- K4ZRC1
- Type
- protein
- Length
- 217 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x7012c0b45c68a2c067644b9d3e5DDa06892c6957
- Molecule
- Pro-pro endopeptidase
- UniProt
- K4ZRC1
- Pockets
- 1 · best druggability 0.57
Structure
1 distinct chain · 44% helix, 7% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Pro-pro endopeptidase | protein | 217 | 44% helix, 7% strand | K4ZRC1 |
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 254 | 0.57 | 0.78 | 27 | empty |
Compared structures
- 6FPC · Structure of the pro-pro endopeptidase (ppep-2) from paenibacillus alvei · an experimental structure of the same protein · chain A against B, TM-score 0.85
- 6FPC · Structure of the PRO-PRO endopeptidase (PPEP-2) from Paenibacillus alvei · an experimental structure of the same protein · chain A against B, TM-score 0.85
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 K4ZRC1
- Elsewhere: UniProt K4ZRC1 · AlphaFold DB K4ZRC1
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.