MolNFT v1 · #183509 · protein
Al amyloid fibril from a lambda 1 light chain
7NSL · Amyloid LAMBDA1 light chain: “Al amyloid fibril from a lambda 1 light chain”. Electron microscopy, 3 pockets (best druggability 0.69). MolNFT v1 #183509 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 7NSL
- Type
- protein
- Length
- 595 residues
- Chains
- 7
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Amyloid LAMBDA1 light chain
- Pockets
- 3 · best druggability 0.69
Structure
electron microscopy · 1 distinct chain · 0% helix, 41% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| D, E, F, C, B, A, G | Amyloid LAMBDA1 light chain | protein | 85 | 0% helix, 41% strand | — |
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 128 | 0.69 | 0.91 | 56 | empty |
| 2 | 54 | 0.60 | 0.92 | 33 | empty |
| 3 | 150 | 0.47 | 0.77 | 32 | empty |
Interfaces
11 interfaces between chains.
- E–F · 3401 Ų buried · 98 hydrogen bonds · protein-protein
- F–G · 3400 Ų buried · 98 hydrogen bonds · protein-protein
- D–E · 3398 Ų buried · 98 hydrogen bonds · protein-protein
- D–C · 3397 Ų buried · 98 hydrogen bonds · protein-protein
- B–A · 3395 Ų buried · 98 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 7 disulfide (disulfide).
Compared structures
- 7NSL · AL amyloid fibril from a lambda 1 light chain · the same entry in another collection · chain D against D, 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 7NSL · PDBe 7NSL
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