Research workbench
AlphaFold monomer V2.0 prediction for protein 4.1 (P11171)
Analyse AlphaFold monomer V2.0 prediction for protein 4.1 (P11171) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P11171
- Type
- protein
- Length
- 864 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xC844D928d873971D6B9E59c8C689034D26A37f39
- UniProt
- P11171
Structure
1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 864 | — | P11171 |
Compared structures
- 1GG3 · Crystal structure of the protein 4.1R membrane binding domain · an experimental structure of the same protein · chain A against A, TM-score 0.32
- 1GG3 · Crystal structure of the protein 4.1R membrane binding domain · an experimental structure of the same protein · chain A against A, TM-score 0.32
- 3QIJ · Primitive-monoclinic crystal structure of the ferm domain of protein 4.1R · an experimental structure of the same protein · chain A against B, TM-score 0.31
- 3QIJ · Primitive-monoclinic crystal structure of the FERM domain of protein 4.1R · an experimental structure of the same protein · chain A against B, TM-score 0.31
- 2RQ1 · Solution structure of the 4.1R FERM alpha lobe domain · an experimental structure of the same protein · chain A against A, TM-score 0.11
- 2RQ1 · Solution structure of the 4.1R ferm alpha lobe domain · an experimental structure of the same protein · chain A against A, TM-score 0.11
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 P11171
- Elsewhere: UniProt P11171 · AlphaFold DB P11171
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