Research workbench
AlphaFold monomer V2.0 prediction for mannosyl-3-phosphoglycerate phosphatase (P76329)
Analyse AlphaFold monomer V2.0 prediction for mannosyl-3-phosphoglycerate phosphatase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P76329
- Type
- protein
- Length
- 271 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x3BB61284E47a075411d99C0E0F0AFdea58cF5CD6
- Molecule
- Mannosyl-3-phosphoglycerate phosphatase
- UniProt
- P76329
- Pockets
- 1 · best druggability 0.70
Structure
1 distinct chain · 41% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Mannosyl-3-phosphoglycerate phosphatase | protein | 271 | 41% helix, 22% strand | P76329 |
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 | 182 | 0.70 | 0.89 | 34 | empty |
Compared structures
- 1XVI · Crystal Structure of YedP, phosphatase-like domain protein from Escherichia coli K12 · an experimental structure of the same protein · chain A against B, TM-score 0.80
- 1XVI · Crystal structure of yedp, phosphatase-like domain protein from escherichia COLI K12 · an experimental structure of the same protein · chain A against B, TM-score 0.80
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 P76329
- Elsewhere: UniProt P76329 · AlphaFold DB P76329
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