Research workbench
Protein folding on a highly rugged landscape: experimental observation of glassy dynamics and structural frustration
Analyse Protein folding on a highly rugged landscape: experimental observation of… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2K6R
- Type
- protein
- Length
- 29 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Full sequence design 1 synthetic superstable
Structure
solution nmr · 1 distinct chain · 38% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Full sequence design 1 synthetic superstable | protein | 29 | 38% helix, 0% strand | — |
Modifications
Observed in the structure: 2 modified (nonstandard).
Compared structures
- 2K6R · Protein folding on a highly rugged landscape: Experimental observation of glassy dynamics… · 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
- Elsewhere: RCSB PDB 2K6R · PDBe 2K6R
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.