Research workbench
Noe-based 3D structure of the predissociated homodimer of CYLR2 in equilibrium with monomer at 266K (-7 celsius degrees)
Analyse Noe-based 3D structure of the predissociated homodimer of CYLR2 in equilibrium… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2LYL
- Type
- protein
- Length
- 132 residues
- Chains
- 2
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- CYLR2
- UniProt
- Q8VL32
Structure
solution nmr · 1 distinct chain · 56% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | CYLR2 | protein | 66 | 56% helix, 0% strand | Q8VL32 |
Interfaces
1 interface between chains.
- A–B · 832 Ų buried · 14 hydrogen bonds · protein-protein
Compared structures
- 2LYL · NOE-based 3D structure of the predissociated homodimer of CylR2 in equilibrium with… · the same entry in another collection · chain A against A, TM-score 1.00
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 Q8VL32
- Elsewhere: RCSB PDB 2LYL · PDBe 2LYL · UniProt Q8VL32
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