Research workbench
Staphylococcus aureus ftsz T7 chimera mutant, T7BS
Analyse Staphylococcus aureus ftsz T7 chimera mutant, T7BS in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3WGJ
- Type
- protein
- Length
- 608 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cell division protein ftsz
- UniProt
- P0A029
- Ligands
- CA
- Pockets
- 7 · best druggability 0.60
Structure
x-ray diffraction · 1 distinct chain · 45% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Cell division protein ftsz | protein | 304 | 45% helix, 24% strand | P0A029 |
Ligands and binding sites
- CA · Calcium ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 261 | 0.60 | 0.80 | 41 | empty |
| 2 | 237 | 0.59 | 0.80 | 41 | empty |
| 3 | 114 | 0.50 | 0.81 | 16 | empty |
| 4 | 121 | 0.50 | 0.80 | 16 | empty |
| 5 | 236 | 0.46 | 0.73 | 35 | empty |
Interfaces
1 interface between chains.
- A–B · 30 Ų buried · 0 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 P0A029
- Elsewhere: RCSB PDB 3WGJ · PDBe 3WGJ · UniProt P0A029
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