Research workbench
P. aeruginosa ftsk motor domain, dimeric
Analyse P. aeruginosa ftsk motor domain, dimeric in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2IUT
- Type
- protein
- Length
- 816 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- DNA translocase ftsk
- UniProt
- Q9I0M3
- Ligands
- AGS, MG
- Pockets
- 7 · best druggability 0.88
Structure
x-ray diffraction · 1 distinct chain · 36% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | DNA translocase ftsk | protein | 408 | 36% helix, 19% strand | Q9I0M3 |
Ligands and binding sites
- AGS · Phosphothiophosphoric acid-adenylate ester · ligand · 2 copies · chains A, B
- MG · Magnesium ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1156 | 0.88 | 0.90 | 138 | AGS, MG |
| 2 | 147 | 0.50 | 0.79 | 28 | empty |
| 3 | 129 | 0.48 | 0.79 | 28 | empty |
| 4 | 62 | 0.41 | 0.82 | 22 | empty |
| 5 | 129 | 0.40 | 0.75 | 21 | empty |
Interfaces
1 interface between chains.
- A–B · 1242 Ų buried · 12 hydrogen bonds · protein-protein
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 Q9I0M3
- Elsewhere: RCSB PDB 2IUT · PDBe 2IUT · UniProt Q9I0M3
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