Research workbench
Crystal structure of RV0371C from mycobacterium tuberculosis H37RV
Analyse Crystal structure of RV0371C from mycobacterium tuberculosis H37RV in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2WE9
- Type
- protein
- Length
- 384 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Moba-related protein
- UniProt
- O53706
- Pockets
- 4 · best druggability 0.67
Structure
x-ray diffraction · 2 distinct chains · 33% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Moba-related protein | protein | 190 | 31% helix, 25% strand | O53706 |
| B | Moba-related protein | protein | 194 | 35% helix, 26% strand | O53706 |
Ligands and binding sites
- GOL · Glycerol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 302 | 0.67 | 0.82 | 38 | empty |
| 2 | 369 | 0.62 | 0.78 | 41 | GOL |
| 3 | 251 | 0.54 | 0.77 | 35 | empty |
| 4 | 72 | 0.36 | 0.77 | 13 | empty |
Interfaces
1 interface between chains.
- A–B · 454 Ų buried · 7 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 7 modified (engineered).
Compared structures
- 2WE9 · Crystal structure of Rv0371c from Mycobacterium tuberculosis H37Rv · 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 O53706
- Elsewhere: RCSB PDB 2WE9 · PDBe 2WE9 · UniProt O53706
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