MolNFT v1 · #150114 · protein
Two protofilament beta-2-microglobulin amyloid fibril
6GK3: “Two protofilament beta-2-microglobulin amyloid fibril”. Electron microscopy, 4 pockets (best druggability 0.62). MolNFT v1 #150114 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6GK3
- Type
- protein
- Length
- 512 residues
- Chains
- 8
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Beta-2-microglobulin
- UniProt
- P61769
- Pockets
- 4 · best druggability 0.62
Structure
electron microscopy · 1 distinct chain · 0% helix, 53% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G, H | Beta-2-microglobulin | protein | 64 | 0% helix, 53% strand | P61769 |
Pockets
4 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 109 | 0.62 | 0.87 | 28 | empty |
| 2 | 111 | 0.61 | 0.86 | 28 | empty |
| 3 | 73 | 0.59 | 0.89 | 24 | empty |
| 4 | 72 | 0.58 | 0.89 | 24 | empty |
Interfaces
16 interfaces between chains.
- A–B · 2918 Ų buried · 78 hydrogen bonds · protein-protein
- B–C · 2917 Ų buried · 79 hydrogen bonds · protein-protein
- E–F · 2916 Ų buried · 78 hydrogen bonds · protein-protein
- F–G · 2915 Ų buried · 79 hydrogen bonds · protein-protein
- C–D · 2914 Ų buried · 82 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 8 disulfide (disulfide).
Compared structures
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 P61769
- Elsewhere: RCSB PDB 6GK3 · PDBe 6GK3 · UniProt P61769
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