Research workbench
Structure of giardia fructose-1,6-biphosphate aldolase
Analyse Structure of giardia fructose-1,6-biphosphate aldolase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3GAK
- Type
- protein
- Length
- 592 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Fructose-bisphosphate aldolase
- EC
- 4.1.2.13
- UniProt
- O97447
- Ligands
- ZN, SO4
- Pockets
- 1 · best druggability 0.48
Structure
x-ray diffraction · 2 distinct chains · 52% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Fructose-bisphosphate aldolase (EC 4.1.2.13) | protein | 290 | 52% helix, 14% strand | O97447 |
| B | Fructose-bisphosphate aldolase (EC 4.1.2.13) | protein | 302 | 51% helix, 14% strand | O97447 |
Ligands and binding sites
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 | 97 | 0.48 | 0.81 | 24 | SO4 |
Interfaces
1 interface between chains.
- A–B · 2159 Ų buried · 26 hydrogen bonds · protein-protein
Compared structures
- 3GAK · Structure of Giardia fructose-1,6-biphosphate aldolase · 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 O97447
- Elsewhere: RCSB PDB 3GAK · PDBe 3GAK · UniProt O97447
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