Research workbench
AlphaFold monomer V2.0 prediction for glutamate racemase (Q5SHT7)
Analyse AlphaFold monomer V2.0 prediction for glutamate racemase (Q5SHT7) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q5SHT7
- Type
- protein
- Length
- 257 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x6Ed09D80e98fE15DE51C9E7a8896AbF1f2365C3e
- Molecule
- Glutamate racemase
- UniProt
- Q5SHT7
Structure
1 distinct chain · 46% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glutamate racemase | protein | 257 | 46% helix, 16% strand | Q5SHT7 |
Compared structures
- 6DLI · Crystal structure of glutamate racemase from Thermus thermophilus in complex with… · an experimental structure of the same protein · chain A against B, TM-score 0.97
- 6DLI · Crystal structure of glutamate racemase from thermus thermophilus in complex with… · an experimental structure of the same protein · chain A against A, TM-score 0.97
- 5W16 · Crystal structure of glutamate racemase from Thermus thermophilus in complex with… · an experimental structure of the same protein · chain A against D, TM-score 0.96
- 5W16 · Crystal structure of glutamate racemase from thermus thermophilus in complex with… · an experimental structure of the same protein · chain A against A, TM-score 0.96
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 Q5SHT7
- Elsewhere: UniProt Q5SHT7 · AlphaFold DB Q5SHT7
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