Research workbench
P. aeruginosa ftsk motor domain, hexamer
Analyse P. aeruginosa ftsk motor domain, hexamer in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2IUU
- Type
- protein
- Length
- 2,448 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- DNA translocase ftsk
- UniProt
- Q9I0M3
- Ligands
- ADP
- Pockets
- 20 · best druggability 0.78
Structure
x-ray diffraction · 1 distinct chain · 38% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F | DNA translocase ftsk | protein | 408 | 38% helix, 20% strand | Q9I0M3 |
Ligands and binding sites
- ADP · Adenosine-5'-diphosphate · ligand · 6 copies · chains A, B, C, D, E, F
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 10 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1080 | 0.78 | 0.80 | 106 | empty |
| 2 | 803 | 0.77 | 0.81 | 92 | empty |
| 3 | 999 | 0.77 | 0.79 | 100 | empty |
| 4 | 995 | 0.77 | 0.79 | 98 | empty |
| 5 | 1103 | 0.77 | 0.79 | 109 | empty |
Interfaces
6 interfaces between chains.
- D–E · 892 Ų buried · 9 hydrogen bonds · protein-protein
- C–D · 891 Ų buried · 10 hydrogen bonds · protein-protein
- E–F · 882 Ų buried · 8 hydrogen bonds · protein-protein
- A–F · 876 Ų buried · 8 hydrogen bonds · protein-protein
- A–B · 867 Ų buried · 8 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 2IUU · PDBe 2IUU · UniProt Q9I0M3
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