Research workbench
Structure, sulfatide-binding properties, and inhibition of platelet aggregation by a disabled-2-derived peptide
Analyse Structure, sulfatide-binding properties, and inhibition of platelet aggregation… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2LSW
- Type
- protein
- Length
- 35 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Disabled homolog 2
- UniProt
- P98082
Structure
solution nmr · 1 distinct chain · 49% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Disabled homolog 2 | protein | 35 | 49% helix, 0% strand | P98082 |
Compared structures
- 2LSW · Structure, sulfatide-binding properties, and inhibition of platelet aggregation by a… · the same entry in another collection · chain A against A, TM-score 1.00
- P98082 · AlphaFold monomer V2.0 prediction for disabled homolog 2 (P98082) · a predicted model of the same protein · chain A against A, TM-score 0.29
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 P98082
- Elsewhere: RCSB PDB 2LSW · PDBe 2LSW · UniProt P98082
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