Research workbench
AlphaFold monomer V2.0 prediction for SERINE/THREONINE-protein phosphatase PGAM5, mitochondrial (Q96HS1)
Analyse AlphaFold monomer V2.0 prediction for SERINE/THREONINE-protein phosphatase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q96HS1
- Type
- protein
- Length
- 289 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x362a6d063b1B7E1B6EfD3A9A7CA3612e3FE037AA
- Molecule
- SERINE/THREONINE-protein phosphatase PGAM5, mitochondrial
- UniProt
- Q96HS1
- Pockets
- 3 · best druggability 0.39
Structure
1 distinct chain · 29% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | SERINE/THREONINE-protein phosphatase PGAM5, mitochondrial | protein | 289 | 29% helix, 14% strand | Q96HS1 |
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 128 | 0.39 | 0.75 | 22 | empty |
| 2 | 53 | 0.39 | 0.81 | 12 | empty |
| 3 | 71 | 0.27 | 0.72 | 16 | empty |
Compared structures
- 5MUF · Crystal structure of human phosphoglycerate mutase family member 5 (PGAM5) in its… · an experimental structure of the same protein · chain A against A, TM-score 0.72
- 5MUF · Crystal structure of human phosphoglycerate mutase family member 5 (PGAM5) in its… · an experimental structure of the same protein · chain A against A, TM-score 0.72
- 6CNL · Crystal Structure of H105A PGAM5 Dodecamer · an experimental structure of the same protein · chain A against L, TM-score 0.66
- 6CNL · Crystal structure of H105A PGAM5 dodecamer · an experimental structure of the same protein · chain A against L, TM-score 0.66
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 Q96HS1
- Elsewhere: UniProt Q96HS1 · AlphaFold DB Q96HS1
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