MolNFT v1 · #34496 · protein
Crystal structure of the ftsh protease domain
2DI4 · Cell division protein ftsh homolog: “Crystal structure of the ftsh protease domain”. X-ray diffraction, 1 ligand (HG), 4 pockets (best druggability 0.60). MolNFT v1 #34496 on GenesisL1: 3D structure, binding sites and pockets in…
- PDB
- 2DI4
- Type
- protein
- Length
- 351 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cell division protein ftsh homolog
- EC
- 3.4.24.-
- UniProt
- O67077
- Ligands
- HG
- Pockets
- 4 · best druggability 0.60
Structure
x-ray diffraction · 2 distinct chains · 66% helix, 3% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cell division protein ftsh homolog (EC 3.4.24.-) | protein | 176 | 67% helix, 3% strand | O67077 |
| B | Cell division protein ftsh homolog (EC 3.4.24.-) | protein | 175 | 64% helix, 3% strand | O67077 |
Ligands and binding sites
- HG · Mercury (II) ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 72 | 0.60 | 0.89 | 19 | empty |
| 2 | 68 | 0.39 | 0.79 | 19 | empty |
| 3 | 108 | 0.36 | 0.74 | 22 | HG |
| 4 | 80 | 0.34 | 0.75 | 14 | empty |
Interfaces
1 interface between chains.
- A–B · 1204 Ų buried · 17 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
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 O67077
- Elsewhere: RCSB PDB 2DI4 · PDBe 2DI4 · UniProt O67077
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