Research workbench
Solution structure and backbone dynamics of a double mutant single- chain MONELLIN(SCM) determined by nuclear magnetic resonance spectroscopy
Analyse Solution structure and backbone dynamics of a double mutant single- chain… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1FUW
- Type
- protein
- Length
- 91 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Monellin
- UniProt
- P02882, P02881
Structure
solution nmr · 1 distinct chain · 14% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Monellin | protein | 91 | 14% helix, 31% strand | P02882, P02881 |
Compared structures
- 1FUW · Solution structure and backbone dynamics of a double mutant single-chain MONELLIN(SCM)… · the same entry in another collection · chain A against A, TM-score 1.00
- P02882 · AlphaFold monomer V2.0 prediction for monellin chain B (P02882) · a predicted model of the same protein · chain A against A, TM-score 0.38
- P02881 · AlphaFold monomer V2.0 prediction for monellin chain a (P02881) · a predicted model of the same protein · chain A against A, TM-score 0.30
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 P02882
- Every structure of UniProt P02881
- Elsewhere: RCSB PDB 1FUW · PDBe 1FUW · UniProt P02882 · UniProt P02881
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