Research workbench
Cross-alpha amyloid-like structure alphatet
Analyse Cross-alpha amyloid-like structure alphatet in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6C52
- Type
- protein
- Length
- 100 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cross-alpha amyloid-like structure alphatet
- Ligands
- ACE, NH2
Structure
x-ray diffraction · 1 distinct chain · 92% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Cross-alpha amyloid-like structure alphatet | protein | 25 | 92% helix, 0% strand | — |
Ligands and binding sites
- ACE · Acetyl group · ligand · 4 copies · chains A, D, B, C
- NH2 · Amino group · ion · 4 copies · chains A, B, C, D
- GOL · Glycerol · additive · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
6 interfaces between chains.
- B–C · 646 Ų buried · 6 hydrogen bonds · protein-protein
- A–B · 602 Ų buried · 4 hydrogen bonds · protein-protein
- C–D · 577 Ų buried · 2 hydrogen bonds · protein-protein
- A–D · 574 Ų buried · 7 hydrogen bonds · protein-protein
- B–D · 166 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 covalent (covalent ligand).
Compared structures
- 6C52 · Cross-alpha Amyloid-like Structure alphaTet · 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 6C52 · PDBe 6C52
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.