Research workbench
NMR identification and characterization of the flexible regions in the 160 kd molten globule-like aggregate of barstar at low pH
Analyse NMR identification and characterization of the flexible regions in the 160 kd… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1L1K
- Type
- protein
- Length
- 20 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Barstar
- UniProt
- P11540
Structure
solution nmr · 1 distinct chain · 0% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Barstar | protein | 20 | 0% helix, 0% strand | P11540 |
Compared structures
- 1L1K · NMR Identification and Characterization of the Flexible Regions in the 160 KD Molten… · the same entry in another collection · chain A against A, TM-score 1.00
- P11540 · AlphaFold monomer V2.0 prediction for barstar (P11540) · a predicted model of the same protein · chain A against A, TM-score 0.17
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 P11540
- Elsewhere: RCSB PDB 1L1K · PDBe 1L1K · UniProt P11540
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