MolNFT v1 · #110462 · protein
L-fuculose 1-phosphate aldolase from glaciozyma antarctica PI12
4XXF · Fuculose-1-phosphate aldolase: “L-fuculose 1-phosphate aldolase from glaciozyma antarctica PI12”. X-ray diffraction, 1 ligand (ZN), 1 pocket (best druggability 0.35). MolNFT v1 #110462 on GenesisL1: 3D structure, binding sites and…
- PDB
- 4XXF
- Type
- protein
- Length
- 249 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Fuculose-1-phosphate aldolase
- EC
- 4.1.2.17
- Ligands
- ZN
- Pockets
- 1 · best druggability 0.35
Structure
x-ray diffraction · 1 distinct chain · 49% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Fuculose-1-phosphate aldolase (EC 4.1.2.17) | protein | 249 | 49% helix, 14% strand | — |
Ligands and binding sites
- ZN · Zinc ion · metal · chains A
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 | 58 | 0.35 | 0.78 | 16 | empty |
Compared structures
- 4XXF · L-fuculose 1-phosphate aldolase from Glaciozyma antarctica PI12 · 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
- Elsewhere: RCSB PDB 4XXF · PDBe 4XXF
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