Research workbench
Mtbetta in the ADP bound state
Analyse Mtbetta in the ADP bound state in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7MU0
- Type
- protein
- Length
- 1,098 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Energy-dependent translational throttle protein etta
- EC
- 3.6.1.-
- UniProt
- P9WQK3
- Ligands
- ADP, MG
- Pockets
- 13 · best druggability 0.77
Structure
x-ray diffraction · 2 distinct chains · 41% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Energy-dependent translational throttle protein etta (EC 3.6.1.-) | protein | 549 | 40% helix, 23% strand | P9WQK3 |
| B | Energy-dependent translational throttle protein etta (EC 3.6.1.-) | protein | 549 | 41% helix, 23% strand | P9WQK3 |
Ligands and binding sites
- ADP · Adenosine-5'-diphosphate · ligand · 4 copies · chains A, B
- MG · Magnesium ion · metal · 4 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
13 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1109 | 0.77 | 0.79 | 129 | MG |
| 2 | 862 | 0.74 | 0.78 | 103 | ADP, MG |
| 3 | 191 | 0.54 | 0.79 | 27 | empty |
| 4 | 85 | 0.49 | 0.83 | 23 | empty |
| 5 | 73 | 0.47 | 0.83 | 19 | empty |
Interfaces
1 interface between chains.
- A–B · 3511 Ų buried · 43 hydrogen bonds · protein-protein
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 P9WQK3
- Elsewhere: RCSB PDB 7MU0 · PDBe 7MU0 · UniProt P9WQK3
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