Research workbench
Lem domain of emerin mutant T43I in complex with baf dimer and the igfold of the lamin A/C
Analyse Lem domain of emerin mutant T43I in complex with baf dimer and the igfold of… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6RPR
- Type
- protein
- Length
- 333 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Prelamin-A/C; Barrier to autointegration factor (baf); Lem domain of emerin mutant T43I
- UniProt
- P02545
- Ligands
- SO4
- Pockets
- 2 · best druggability 0.37
Structure
x-ray diffraction · 3 distinct chains · 34% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B | Prelamin-A/C | protein | 116 | 3% helix, 50% strand | P02545 |
| D, E | Barrier to autointegration factor (baf) | protein | 87 | 68% helix, 2% strand | — |
| G | Lem domain of emerin mutant T43I | protein | 43 | 51% helix, 0% strand | — |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 3 copies · chains D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 118 | 0.37 | 0.74 | 21 | empty |
| 2 | 64 | 0.33 | 0.76 | 13 | empty |
Interfaces
5 interfaces between chains.
- D–E · 761 Ų buried · 8 hydrogen bonds · protein-protein
- D–G · 438 Ų buried · 7 hydrogen bonds · protein-protein
- B–D · 301 Ų buried · 6 hydrogen bonds · protein-protein
- E–G · 300 Ų buried · 2 hydrogen bonds · protein-protein
- B–E · 215 Ų buried · 2 hydrogen bonds · protein-protein
Compared structures
- 6RPR · LEM domain of Emerin mutant T43I in complex with BAF dimer and the Igfold of the lamin A/C · the same entry in another collection · chain B against B, TM-score 1.00
- P02545 · AlphaFold monomer V2.0 prediction for prelamin-A/C (P02545) · a predicted model of the same protein · chain B against A, TM-score 0.99
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 6RPR · PDBe 6RPR · UniProt P02545
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