Research workbench
NMR solution structure of phospholipase C epsilon ra 2 domain
Analyse NMR solution structure of phospholipase C epsilon ra 2 domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2BYF
- Type
- protein
- Length
- 116 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Phospholipase C, epsilon 1
- UniProt
- Q5VWL5
Structure
solution nmr · 1 distinct chain · 21% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phospholipase C, epsilon 1 | protein | 116 | 21% helix, 28% strand | Q5VWL5 |
Compared structures
- 2BYF · NMR solution structure of phospholipase c epsilon RA 2 domain · 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 Q5VWL5
- Elsewhere: RCSB PDB 2BYF · PDBe 2BYF · UniProt Q5VWL5
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