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Mycobacterium tuberculosis ftsz in complex with GDP
Analyse Mycobacterium tuberculosis ftsz in complex with GDP in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6YM1
- Type
- protein
- Length
- 594 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cell division protein ftsz
- UniProt
- P9WN94
- Ligands
- GDP
- Pockets
- 5 · best druggability 0.70
Structure
x-ray diffraction · 2 distinct chains · 45% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cell division protein ftsz | protein | 298 | 47% helix, 25% strand | P9WN94 |
| B | Cell division protein ftsz | protein | 296 | 44% helix, 25% strand | P9WN94 |
Ligands and binding sites
- GDP · Guanosine-5'-diphosphate · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 388 | 0.70 | 0.82 | 52 | empty |
| 2 | 235 | 0.55 | 0.78 | 30 | empty |
| 3 | 194 | 0.54 | 0.78 | 29 | empty |
| 4 | 134 | 0.46 | 0.78 | 29 | GDP |
| 5 | 132 | 0.39 | 0.74 | 30 | empty |
Interfaces
1 interface between chains.
- A–B · 1041 Ų buried · 17 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 P9WN94
- Elsewhere: RCSB PDB 6YM1 · PDBe 6YM1 · UniProt P9WN94
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