Research workbench
Crystal structure of mycobacterium tuberculosis nusa
Analyse Crystal structure of mycobacterium tuberculosis nusa in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1K0R
- Type
- protein
- Length
- 652 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Nusa
- UniProt
- P0A5M2
- Ligands
- SO4
- Pockets
- 4 · best druggability 0.62
Structure
x-ray diffraction · 1 distinct chain · 26% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Nusa | protein | 326 | 26% helix, 24% strand | P0A5M2 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 4 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 360 | 0.62 | 0.78 | 35 | empty |
| 2 | 74 | 0.39 | 0.78 | 22 | empty |
| 3 | 52 | 0.35 | 0.79 | 12 | empty |
| 4 | 75 | 0.33 | 0.75 | 19 | empty |
Interfaces
1 interface between chains.
- A–B · 928 Ų buried · 15 hydrogen bonds · protein-protein
Compared structures
- 1K0R · Crystal Structure of Mycobacterium tuberculosis NusA · 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 P0A5M2
- Elsewhere: RCSB PDB 1K0R · PDBe 1K0R · UniProt P0A5M2
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