Research workbench
Mub is an aaaplus ATPase that forms helical filaments to control target selection for DNA transposition
Analyse Mub is an aaaplus ATPase that forms helical filaments to control target… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4BS1
- Type
- protein
- Length
- 246 residues
- Chains
- 2
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Transcriptional regulator (ntrc family)
- Ligands
- ADP
- Pockets
- 3 · best druggability 0.46
Structure
electron microscopy · 2 distinct chains · 43% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Transcriptional regulator (ntrc family) | protein | 73 | 63% helix, 5% strand | — |
| B | Transcriptional regulator (ntrc family) | protein | 173 | 35% helix, 17% strand | — |
Ligands and binding sites
- ADP · Adenosine-5'-diphosphate · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 116 | 0.46 | 0.78 | 21 | empty |
| 2 | 141 | 0.44 | 0.76 | 26 | empty |
| 3 | 59 | 0.39 | 0.80 | 13 | empty |
Interfaces
1 interface between chains.
- A–B · 621 Ų buried · 6 hydrogen bonds · protein-protein
Compared structures
- 4BS1 · MuB is an AAAplus ATPase that forms helical filaments to control target selection for DNA… · 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
- Elsewhere: RCSB PDB 4BS1 · PDBe 4BS1
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