Research workbench
Ftsz, T7 mutated, domain swapped (T. maritima)
Analyse Ftsz, T7 mutated, domain swapped (T. maritima) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1W5F
- Type
- protein
- Length
- 630 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cell division protein ftsz
- UniProt
- O08398
- Ligands
- G2P, MG
- Pockets
- 8 · best druggability 0.76
Structure
x-ray diffraction · 1 distinct chain · 44% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Cell division protein ftsz | protein | 315 | 44% helix, 23% strand | O08398 |
Ligands and binding sites
- G2P · Phosphomethylphosphonic acid guanylate ester · 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
8 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 455 | 0.76 | 0.85 | 59 | empty |
| 2 | 98 | 0.73 | 0.94 | 31 | empty |
| 3 | 134 | 0.62 | 0.86 | 20 | empty |
| 4 | 165 | 0.62 | 0.84 | 24 | empty |
| 5 | 119 | 0.60 | 0.86 | 20 | empty |
Interfaces
1 interface between chains.
- A–B · 3980 Ų buried · 49 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 O08398
- Elsewhere: RCSB PDB 1W5F · PDBe 1W5F · UniProt O08398
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