MolNFT v1 · #3387 · protein
Protein aggregation and ALZHEIMER'S disease: crystallographic analysis of the phenomenon. engineered version of the ribosomal protein S6 used as a stable scaffold to study oligomerization.
1CQM: “Protein aggregation and ALZHEIMER'S disease: crystallographic analysis of the phenomenon. engineered version…”. X-ray diffraction. MolNFT v1 #3387 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1CQM
- Type
- protein
- Length
- 196 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P23370
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | — | protein | 98 | — | P23370 |
Compared structures
- 1CQM · Protein aggregation and ALZHEIMER'S disease: crystallographic analysis of the phenomenon.… · 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 P23370
- Elsewhere: RCSB PDB 1CQM · PDBe 1CQM · UniProt P23370
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