Research workbench
AlphaFold monomer V2.0 prediction for probable inactive ATP-dependent zinc metalloprotease ftshi 2, chloroplastic (A8MPR5)
Analyse AlphaFold monomer V2.0 prediction for probable inactive ATP-dependent zinc… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A8MPR5
- Type
- protein
- Length
- 876 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xd1A2963012bEcbC7A8f505464439Ab678C48936f
- UniProt
- A8MPR5
Structure
1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 876 | — | A8MPR5 |
Compared structures
- 8XKV · Cryo-EM structure of the Ycf2-FtsHi motor complex from Arabidopsis in Apo state · an experimental structure of the same protein · chain A against F, TM-score 0.50
- 8XKU · Cryo-EM structure of the Ycf2-FtsHi motor complex from Arabidopsis in ATP-bound state · an experimental structure of the same protein · chain A against F, TM-score 0.49
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 A8MPR5
- Elsewhere: UniProt A8MPR5 · AlphaFold DB A8MPR5
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