Research workbench
AlphaFold monomer V2.0 prediction for methionine import ATP-binding protein metn (Q87RS1)
Analyse AlphaFold monomer V2.0 prediction for methionine import ATP-binding protein… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q87RS1
- Type
- protein
- Length
- 344 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x4Ef77Afb5a3D9F41c95Be3227D1CC986CCb61835
- UniProt
- Q87RS1
Structure
1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 344 | — | Q87RS1 |
Compared structures
- 2QRR · Crystal structure of the soluble domain of the ABC transporter, ATP-binding protein from… · an experimental structure of the same protein · chain A against B, TM-score 0.27
- 2QRR · Crystal structure of the soluble domain of the ABC transporter, ATP- binding protein from… · an experimental structure of the same protein · chain A against B, TM-score 0.27
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 Q87RS1
- Elsewhere: UniProt Q87RS1 · AlphaFold DB Q87RS1
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