Research workbench
complete structure of the Mycobacterium tuberculosis proteasomal ATPase Mpa
Analyse complete structure of the Mycobacterium tuberculosis proteasomal ATPase Mpa in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5KWA
- Type
- protein
- Length
- 908 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.9
- Source
- Mycobacterium tuberculosis
- Molecule
- Proteasome-associated ATPase
- UniProt
- A0A0T9XQP1
- Ligands
- ADP, MG
- Pockets
- 10 · best druggability 0.81
Structure
x-ray diffraction · resolution 2.9 · 1 distinct chain · 37% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Proteasome-associated ATPase | protein | 454 | 37% helix, 24% strand | A0A0T9XQP1 |
Ligands and binding sites
- ADP · Adenosine-5'-diphosphate · ligand · 2 copies · chains A, B
- MG · Magnesium ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
10 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1045 | 0.81 | 0.82 | 112 | ADP, MG |
| 2 | 504 | 0.70 | 0.80 | 44 | empty |
| 3 | 516 | 0.69 | 0.79 | 53 | empty |
| 4 | 388 | 0.60 | 0.76 | 51 | empty |
| 5 | 101 | 0.59 | 0.87 | 21 | empty |
Interfaces
1 interface between chains.
- A–B · 2631 Ų buried · 42 hydrogen bonds · protein-protein
Compared structures
- 5KWA · Complete structure of the mycobacterium tuberculosis proteasomal ATPase mpa · 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 A0A0T9XQP1
- Elsewhere: RCSB PDB 5KWA · PDBe 5KWA · UniProt A0A0T9XQP1
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