Research workbench
Structure of the N-terminal domain of Wag31
Analyse Structure of the N-terminal domain of Wag31 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6LFA
- Type
- protein
- Length
- 132 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.3
- Source
- Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
- Molecule
- Cell wall synthesis protein Wag31
- UniProt
- P9WMU1
- Pockets
- 1 · best druggability 0.31
Structure
x-ray diffraction · resolution 2.3 · 2 distinct chains · 61% helix, 2% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cell wall synthesis protein Wag31 | protein | 70 | 59% helix, 1% strand | P9WMU1 |
| B | Cell wall synthesis protein Wag31 | protein | 62 | 65% helix, 2% strand | P9WMU1 |
Ligands and binding sites
- PGE · Triethylene glycol · additive · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 68 | 0.31 | 0.74 | 14 | empty |
Interfaces
1 interface between chains.
- A–B · 2078 Ų buried · 31 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 P9WMU1
- Elsewhere: RCSB PDB 6LFA · PDBe 6LFA · UniProt P9WMU1
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