Research workbench
Crystal structure of lprg from mycobacterium tuberculosis
Analyse Crystal structure of lprg from mycobacterium tuberculosis in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3MH8
- Type
- protein
- Length
- 390 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Lipoprotein lprg
- UniProt
- P0A5I8
- Pockets
- 3 · best druggability 0.80
Structure
x-ray diffraction · 2 distinct chains · 18% helix, 48% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Lipoprotein lprg | protein | 196 | 19% helix, 48% strand | P0A5I8 |
| B | Lipoprotein lprg | protein | 194 | 18% helix, 47% strand | P0A5I8 |
Pockets
3 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 530 | 0.80 | 0.86 | 51 | empty |
| 2 | 434 | 0.75 | 0.83 | 52 | empty |
| 3 | 782 | 0.70 | 0.77 | 81 | empty |
Interfaces
1 interface between chains.
- A–B · 391 Ų buried · 9 hydrogen bonds · protein-protein
Compared structures
- 3MH8 · Crystal structure of LprG from Mycobacterium tuberculosis · 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 P0A5I8
- Elsewhere: RCSB PDB 3MH8 · PDBe 3MH8 · UniProt P0A5I8
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