Research workbench
AlphaFold monomer V2.0 prediction for cadherin-3 (P10287)
Analyse AlphaFold monomer V2.0 prediction for cadherin-3 (P10287) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P10287
- Type
- protein
- Length
- 822 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x7012c0b45c68a2c067644b9d3e5DDa06892c6957
- UniProt
- P10287
Structure
1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 822 | — | P10287 |
Compared structures
- 4NQQ · Crystal structure of mouse P-cadherin extracellular domains EC1-EC2 · an experimental structure of the same protein · chain A against C, TM-score 0.25
- 4NQQ · Crystal structure of mouse P-cadherin extracellular domains EC1-EC2 · an experimental structure of the same protein · chain A against C, TM-score 0.25
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 P10287
- Elsewhere: UniProt P10287 · AlphaFold DB P10287
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