Research workbench
Crystal structure of the ftsh ATPase domain from thermus thermophilus
Analyse Crystal structure of the ftsh ATPase domain from thermus thermophilus in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1IXZ
- Type
- protein
- Length
- 238 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- ATP-dependent metalloprotease ftsh
- UniProt
- Q9LCZ4
- Ligands
- HG, SO4
- Pockets
- 2 · best druggability 0.48
Structure
x-ray diffraction · 1 distinct chain · 52% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ATP-dependent metalloprotease ftsh | protein | 238 | 52% helix, 12% strand | Q9LCZ4 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 141 | 0.48 | 0.78 | 38 | HG, SO4 |
| 2 | 69 | 0.45 | 0.82 | 19 | empty |
Compared structures
- 1IXZ · Crystal structure of the FtsH ATPase domain from Thermus thermophilus · 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 Q9LCZ4
- Elsewhere: RCSB PDB 1IXZ · PDBe 1IXZ · UniProt Q9LCZ4
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