Research workbench
S. aureus ftsz 12-316 T66W GTP closed form (2TCM)
Analyse S. aureus ftsz 12-316 T66W GTP closed form (2TCM) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5MN5
- Type
- protein
- Length
- 578 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cell division protein ftsz
- UniProt
- P0A031
- Ligands
- GTP
- Pockets
- 8 · best druggability 0.75
Structure
x-ray diffraction · 2 distinct chains · 46% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cell division protein ftsz | protein | 292 | 45% helix, 24% strand | P0A031 |
| B | Cell division protein ftsz | protein | 286 | 46% helix, 25% strand | P0A031 |
Ligands and binding sites
- GTP · Guanosine-5'-triphosphate · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 617 | 0.75 | 0.81 | 69 | empty |
| 2 | 137 | 0.48 | 0.79 | 24 | GTP |
| 3 | 122 | 0.48 | 0.79 | 25 | GTP |
| 4 | 78 | 0.47 | 0.83 | 17 | empty |
| 5 | 53 | 0.45 | 0.85 | 14 | empty |
Interfaces
1 interface between chains.
- A–B · 744 Ų buried · 8 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 P0A031
- Elsewhere: RCSB PDB 5MN5 · PDBe 5MN5 · UniProt P0A031
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