Research workbench
Saftsz-UCM152 (COMP.20)
Analyse Saftsz-UCM152 (COMP.20) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6YD6
- 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, OMW, MB3, K
- Pockets
- 3 · best druggability 0.66
Structure
x-ray diffraction · 1 distinct chain · 43% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cell division protein ftsz | protein | 307 | 43% helix, 23% strand | P0A031 |
Ligands and binding sites
- GDP · Guanosine-5'-diphosphate · ligand · chains A
- OMW · 2,6-bis(fluoranyl)-3-[[3-(trifluoromethyl) phenyl]methoxy]benzamide · ligand · chains A
- MB3 · 1-methylpyrrolidin-2-one · ligand · chains A
- K · Potassium ion · metal · chains A
- EDO · 1,2-ethanediol · additive · 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, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 165 | 0.66 | 0.86 | 26 | OMW |
| 2 | 211 | 0.60 | 0.81 | 39 | GDP, MB3 |
| 3 | 93 | 0.47 | 0.80 | 16 | 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 6YD6 · PDBe 6YD6 · UniProt P0A031
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