Research workbench
AlphaFold monomer V2.0 prediction for maintenance of mitochondrial morphology protein 1 (C5DRQ1)
Analyse AlphaFold monomer V2.0 prediction for maintenance of mitochondrial morphology… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- C5DRQ1
- Type
- protein
- Length
- 454 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x7a1388B6Aad67B04634A32f63b8A6D6005eab86c
- UniProt
- C5DRQ1
Structure
1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 454 | — | C5DRQ1 |
Compared structures
- 5YK6 · Crystal structure of MMM1 · an experimental structure of the same protein · chain A against A, TM-score 0.52
- 5YK6 · Crystal Structure of Mmm1 · an experimental structure of the same protein · chain A against A, TM-score 0.52
- 5YK7 · Crystal structure of MDM12-MMM1 complex · an experimental structure of the same protein · chain A against A, TM-score 0.46
- 5YK7 · Crystal Structure of Mdm12-Mmm1 complex · an experimental structure of the same protein · chain A against A, TM-score 0.46
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 C5DRQ1
- Elsewhere: UniProt C5DRQ1 · AlphaFold DB C5DRQ1
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