MolNFT v1 · #83386 · protein
Staphylococcus aureus ftsz T7 mutant substituted for gan bound with GTP, DELTAT7GAN-GTP
3WGM · Cell division protein ftsz: “Staphylococcus aureus ftsz T7 mutant substituted for gan bound with GTP, DELTAT7GAN-GTP”. X-ray diffraction, 2 ligands (GTP, MG), 6 pockets (best druggability 0.70). MolNFT v1 #83386 on GenesisL1: 3D…
- PDB
- 3WGM
- Type
- protein
- Length
- 602 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cell division protein ftsz
- UniProt
- P0A029
- Ligands
- GTP, MG
- Pockets
- 6 · best druggability 0.70
Structure
x-ray diffraction · 1 distinct chain · 46% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Cell division protein ftsz | protein | 301 | 46% helix, 24% strand | P0A029 |
Ligands and binding sites
- GTP · Guanosine-5'-triphosphate · ligand · 2 copies · chains A, B
- MG · Magnesium ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 634 | 0.70 | 0.78 | 51 | empty |
| 2 | 255 | 0.61 | 0.80 | 35 | empty |
| 3 | 248 | 0.60 | 0.80 | 33 | empty |
| 4 | 209 | 0.59 | 0.81 | 41 | GTP, MG |
| 5 | 211 | 0.58 | 0.80 | 41 | GTP, MG |
Interfaces
1 interface between chains.
- A–B · 731 Ų buried · 8 hydrogen bonds · protein-protein
Compared structures
- 3WGM · STAPHYLOCOCCUS AUREUS FTSZ T7 mutant substituted for GAN bound with GTP, DeltaT7GAN-GTP · the same entry in another collection · chain B against B, TM-score 1.00
- P0A029 · AlphaFold monomer V2.0 prediction for cell division protein ftsz (P0A029) · a predicted model of the same protein · chain A against A, TM-score 0.87
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 3WGM · PDBe 3WGM · UniProt P0A029
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