Research workbench
Crystal structure of mtiswi
Analyse Crystal structure of mtiswi in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5JXR
- Type
- protein
- Length
- 1,250 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Chromatin-remodeling complex ATPase-like protein
- UniProt
- G2QFM3
- Ligands
- CL
- Pockets
- 17 · best druggability 0.83
Structure
x-ray diffraction · 1 distinct chain · 52% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Chromatin-remodeling complex ATPase-like protein | protein | 625 | 52% helix, 11% strand | G2QFM3 |
Ligands and binding sites
- CL · Chloride ion · ion · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
17 pockets found on a 1 Å grid, 14 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 605 | 0.83 | 0.88 | 78 | empty |
| 2 | 195 | 0.74 | 0.90 | 45 | empty |
| 3 | 479 | 0.74 | 0.83 | 52 | empty |
| 4 | 479 | 0.74 | 0.83 | 49 | empty |
| 5 | 446 | 0.72 | 0.83 | 54 | empty |
Interfaces
1 interface between chains.
- A–B · 5764 Ų buried · 47 hydrogen bonds · protein-protein
Compared structures
- 5JXR · Crystal structure of MtISWI · the same entry in another collection · chain A against A, 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
- Every structure of UniProt G2QFM3
- Elsewhere: RCSB PDB 5JXR · PDBe 5JXR · UniProt G2QFM3
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.