Research workbench
AlphaFold monomer V2.0 prediction for glucosylglycerol phosphorylase (E4PMA5)
Analyse AlphaFold monomer V2.0 prediction for glucosylglycerol phosphorylase (E4PMA5) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- E4PMA5
- Type
- protein
- Length
- 480 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x1392B753cF15F20A431316F678bC32DC3F16C559
- UniProt
- E4PMA5
Structure
1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 480 | — | E4PMA5 |
Compared structures
- 7XDR · Crystal structure of a glucosylglycerol phosphorylase from Marinobacter adhaerens · an experimental structure of the same protein · chain A against F, TM-score 0.98
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 E4PMA5
- Elsewhere: UniProt E4PMA5 · AlphaFold DB E4PMA5
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