Research workbench
Amyloid-related segment of alphab-crystallin residues 90-100 with G95W mutation, bromo derivative
Analyse Amyloid-related segment of alphab-crystallin residues 90-100 with G95W… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7ROL
- Type
- protein
- Length
- 22 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Alpha-crystallin B chain peptide
Structure
x-ray diffraction · 1 distinct chain · 0% helix, 36% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Alpha-crystallin B chain peptide | protein | 11 | 0% helix, 36% strand | — |
Interfaces
1 interface between chains.
- A–B · 547 Ų buried · 16 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 modified (nonstandard).
Compared structures
- 7ROL · Amyloid-related segment of alphaB-crystallin residues 90-100 with G95W mutation, bromo… · 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 7ROL · PDBe 7ROL
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.