Research workbench
Apo FUTA2 from synechocystis PCC6803
Analyse Apo FUTA2 from synechocystis PCC6803 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2VOZ
- Type
- protein
- Length
- 628 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Periplasmic iron-binding protein
- UniProt
- Q55835
- Ligands
- SO4
- Pockets
- 3 · best druggability 0.75
Structure
x-ray diffraction · 2 distinct chains · 46% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Periplasmic iron-binding protein | protein | 313 | 46% helix, 18% strand | Q55835 |
| B | Periplasmic iron-binding protein | protein | 315 | 46% helix, 18% strand | Q55835 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 3 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1089 | 0.75 | 0.77 | 92 | SO4 |
| 2 | 54 | 0.28 | 0.75 | 20 | empty |
| 3 | 51 | 0.25 | 0.73 | 18 | empty |
Interfaces
1 interface between chains.
- A–B · 1246 Ų buried · 27 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 Q55835
- Elsewhere: RCSB PDB 2VOZ · PDBe 2VOZ · UniProt Q55835
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