Research workbench
AlphaFold monomer V2.0 prediction for zinc metalloproteinase- disintegrin-like lachestatin-1 (C5H5D5)
Analyse AlphaFold monomer V2.0 prediction for zinc metalloproteinase- disintegrin-like… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- C5H5D5
- Type
- protein
- Length
- 421 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xfA417B18af2a1c4a3E1bB0F48Eb0f4f629972ce1
- Molecule
- Zinc metalloproteinase-disintegrin-like lachestatin-1
- UniProt
- C5H5D5
- Pockets
- 4 · best druggability 0.57
Structure
1 distinct chain · 27% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Zinc metalloproteinase-disintegrin-like lachestatin-1 | protein | 421 | 27% helix, 19% strand | C5H5D5 |
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 115 | 0.57 | 0.84 | 25 | empty |
| 2 | 333 | 0.56 | 0.75 | 46 | empty |
| 3 | 53 | 0.29 | 0.75 | 11 | empty |
| 4 | 51 | 0.29 | 0.75 | 14 | empty |
Modifications
Observed in the structure: 17 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 C5H5D5
- Elsewhere: UniProt C5H5D5 · AlphaFold DB C5H5D5
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