Research workbench
Crystal structure of the ftsh ATPase domain with ADP from thermus thermophilus
Analyse Crystal structure of the ftsh ATPase domain with ADP 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
- 1IY1
- Type
- protein
- Length
- 234 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- ATP-dependent metalloprotease ftsh
- UniProt
- Q9LCZ4
- Ligands
- ADP
- Pockets
- 1 · best druggability 0.49
Structure
x-ray diffraction · 1 distinct chain · 50% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ATP-dependent metalloprotease ftsh | protein | 234 | 50% helix, 12% strand | Q9LCZ4 |
Ligands and binding sites
- ADP · Adenosine-5'-diphosphate · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 162 | 0.49 | 0.78 | 36 | ADP |
Compared structures
- 1IY1 · Crystal structure of the FtsH ATPase domain with ADP 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 1IY1 · PDBe 1IY1 · UniProt Q9LCZ4
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