Research workbench
AlphaFold monomer V2.0 prediction for GDP-mannose 4,6 dehydratase 2 (P93031)
Analyse AlphaFold monomer V2.0 prediction for GDP-mannose 4,6 dehydratase 2 (P93031) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P93031
- Type
- protein
- Length
- 373 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xc0F878C3f3E2a1874e2A6daC80d429e553DdB0D5
- UniProt
- P93031
Structure
1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 373 | — | P93031 |
Compared structures
- 1N7G · Crystal structure of the GDP-mannose 4,6-dehydratase ternary complex with NADPH and… · an experimental structure of the same protein · chain A against B, TM-score 0.89
- 1N7G · Crystal Structure of the GDP-mannose 4,6-dehydratase ternary complex with NADPH and… · an experimental structure of the same protein · chain A against B, TM-score 0.89
- 1N7H · Crystal structure of GDP-mannose 4,6-dehydratase ternary complex with NADPH and GDP · an experimental structure of the same protein · chain A against B, TM-score 0.89
- 1N7H · Crystal Structure of GDP-mannose 4,6-dehydratase ternary complex with NADPH and GDP · an experimental structure of the same protein · chain A against B, TM-score 0.89
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 P93031
- Elsewhere: UniProt P93031 · AlphaFold DB P93031
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