Research workbench
AlphaFold monomer V2.0 prediction for glycerophosphodiester phosphodiesterase, periplasmic (P09394)
Analyse AlphaFold monomer V2.0 prediction for glycerophosphodiester phosphodiesterase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P09394
- Type
- protein
- Length
- 358 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x30488FCE67dA9Caf3db45ae4Df6F96d4CcFF8672
- UniProt
- P09394
Structure
1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 358 | — | P09394 |
Compared structures
- 1T8Q · Structural genomics, crystal structure of glycerophosphoryl diester phosphodiesterase… · an experimental structure of the same protein · chain A against B, TM-score 0.92
- 1T8Q · Structural genomics, Crystal structure of Glycerophosphoryl diester phosphodiesterase… · an experimental structure of the same protein · chain A against B, TM-score 0.92
- 1YDY · Crystal structure of periplasmic glycerophosphodiester phosphodiesterase from escherichia… · an experimental structure of the same protein · chain A against A, TM-score 0.91
- 1YDY · Crystal structure of periplasmic glycerophosphodiester phosphodiesterase from Escherichia… · an experimental structure of the same protein · chain A against A, TM-score 0.91
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 P09394
- Elsewhere: UniProt P09394 · AlphaFold DB P09394
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