Research workbench
Crystal structure of the R482W mutant of lamin A/C
Analyse Crystal structure of the R482W mutant of lamin A/C in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3GEF
- Type
- protein
- Length
- 472 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.5
- Source
- Homo sapiens
- Molecule
- Lamin-A/C
- UniProt
- P02545
- Pockets
- 1 · best druggability 0.73
Structure
x-ray diffraction · resolution 1.5 · 1 distinct chain · 3% helix, 50% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Lamin-A/C | protein | 118 | 3% helix, 50% strand | P02545 |
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 953 | 0.73 | 0.77 | 95 | empty |
Interfaces
6 interfaces between chains.
- A–B · 879 Ų buried · 21 hydrogen bonds · protein-protein
- C–D · 834 Ų buried · 18 hydrogen bonds · protein-protein
- B–D · 448 Ų buried · 5 hydrogen bonds · protein-protein
- A–C · 433 Ų buried · 5 hydrogen bonds · protein-protein
- A–D · 149 Ų buried · 4 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 modified (oxidation).
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 P02545
- Elsewhere: RCSB PDB 3GEF · PDBe 3GEF · UniProt P02545
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.