Research workbench
Saftsz complexed with GDP and BEF3-
Analyse Saftsz complexed with GDP and BEF3- in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7OHH
- Type
- protein
- Length
- 307 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cell division protein ftsz
- UniProt
- P0A031
- Ligands
- GDP, BEF, K
- Pockets
- 3 · best druggability 0.62
Structure
x-ray diffraction · 1 distinct chain · 45% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cell division protein ftsz | protein | 307 | 45% helix, 24% strand | P0A031 |
Ligands and binding sites
- GDP · Guanosine-5'-diphosphate · ligand · chains A
- BEF · Beryllium trifluoride ion · ligand · chains A
- K · Potassium ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 226 | 0.62 | 0.82 | 39 | GDP, BEF |
| 2 | 86 | 0.45 | 0.80 | 18 | empty |
| 3 | 74 | 0.36 | 0.76 | 14 | empty |
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 7OHH · PDBe 7OHH · UniProt P0A031
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