Research workbench
Structure of F-actin binding domain imd of mim (missing in metastasis)
Analyse Structure of F-actin binding domain imd of mim (missing in metastasis) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2D1L
- Type
- protein
- Length
- 480 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Metastasis suppressor protein 1
- UniProt
- Q8R1S4
- Pockets
- 3 · best druggability 0.88
Structure
x-ray diffraction · 2 distinct chains · 89% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Metastasis suppressor protein 1 | protein | 249 | 90% helix, 0% strand | Q8R1S4 |
| B | Metastasis suppressor protein 1 | protein | 231 | 89% helix, 0% strand | Q8R1S4 |
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 383 | 0.88 | 0.96 | 42 | empty |
| 2 | 59 | 0.42 | 0.82 | 16 | empty |
| 3 | 51 | 0.25 | 0.73 | 17 | empty |
Interfaces
1 interface between chains.
- A–B · 3250 Ų buried · 25 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 18 modified (engineered).
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 Q8R1S4
- Elsewhere: RCSB PDB 2D1L · PDBe 2D1L · UniProt Q8R1S4
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