Research workbench
Candida albicans fructose-1,6-bisphosphate aldolase
Analyse Candida albicans fructose-1,6-bisphosphate aldolase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6LNK
- Type
- protein
- Length
- 673 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
- Q9URB4
- Ligands
- ZN
- Pockets
- 6 · best druggability 0.71
Structure
x-ray diffraction · 2 distinct chains · 51% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Fructose-bisphosphate aldolase (EC 4.1.2.13) | protein | 336 | 50% helix, 12% strand | Q9URB4 |
| B | Fructose-bisphosphate aldolase (EC 4.1.2.13) | protein | 337 | 52% helix, 13% strand | Q9URB4 |
Ligands and binding sites
- ZN · Zinc ion · metal · 2 copies · chains A, B
- EDO · 1,2-ethanediol · additive · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 117 | 0.71 | 0.91 | 24 | empty |
| 2 | 222 | 0.53 | 0.77 | 35 | empty |
| 3 | 198 | 0.52 | 0.78 | 33 | empty |
| 4 | 238 | 0.47 | 0.73 | 31 | EDO |
| 5 | 97 | 0.37 | 0.75 | 23 | empty |
Interfaces
1 interface between chains.
- A–B · 2163 Ų buried · 23 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 Q9URB4
- Elsewhere: RCSB PDB 6LNK · PDBe 6LNK · UniProt Q9URB4
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