Research workbench
Solution structure of the fifth ig-like domain from human roundabout homolog 2
Analyse Solution structure of the fifth ig-like domain from human roundabout homolog 2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2EDJ
- Type
- protein
- Length
- 100 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Roundabout homolog 2
- UniProt
- Q9HCK4
Structure
solution nmr · 1 distinct chain · 0% helix, 43% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Roundabout homolog 2 | protein | 100 | 0% helix, 43% strand | Q9HCK4 |
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 2EDJ · Solution structure of the fifth ig-like domain from human Roundabout homolog 2 · the same entry in another collection · chain A against A, TM-score 1.00
- Q9HCK4 · AlphaFold monomer V2.0 prediction for roundabout homolog 2 (Q9HCK4) · a predicted model of the same protein · chain A against A, TM-score 0.90
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 Q9HCK4
- Elsewhere: RCSB PDB 2EDJ · PDBe 2EDJ · UniProt Q9HCK4
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