Research workbench
Crystal structure of kpftsz (residues 11-316)
Analyse Crystal structure of kpftsz (residues 11-316) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6LL5
- Type
- protein
- Length
- 306 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cell division protein ftsz
- UniProt
- W9BCK7
- Ligands
- GDP
- Pockets
- 4 · best druggability 0.48
Structure
x-ray diffraction · 1 distinct chain · 47% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cell division protein ftsz | protein | 306 | 47% helix, 25% strand | W9BCK7 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 133 | 0.48 | 0.79 | 30 | GDP |
| 2 | 175 | 0.46 | 0.75 | 25 | empty |
| 3 | 77 | 0.32 | 0.74 | 18 | empty |
| 4 | 57 | 0.30 | 0.76 | 15 | empty |
Compared structures
- 6LL5 · Crystal structure of KpFtsZ (residues 11-316) · the same entry in another collection · chain A against A, TM-score 1.00
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 W9BCK7
- Elsewhere: RCSB PDB 6LL5 · PDBe 6LL5 · UniProt W9BCK7
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