Research workbench
L-fuculose-1-phosphate aldolase complex with pgh
Analyse L-fuculose-1-phosphate aldolase complex with pgh in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4FUA
- Type
- protein
- Length
- 206 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- L-fuculose-1-phosphate aldolase
- EC
- 4.1.2.17
- UniProt
- P0AB87
- Ligands
- PGH, ZN, SO4
- Pockets
- 1 · best druggability 0.55
Structure
x-ray diffraction · 1 distinct chain · 42% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | L-fuculose-1-phosphate aldolase (EC 4.1.2.17) | protein | 206 | 42% helix, 17% strand | P0AB87 |
Ligands and binding sites
- PGH · Phosphoglycolohydroxamic acid · ligand · chains A
- ZN · Zinc ion · metal · chains A
- SO4 · Sulfate ion · ion · chains A
- BME · Beta-mercaptoethanol · additive · 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, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 94 | 0.55 | 0.85 | 25 | ZN, BME, PGH |
Modifications
Observed in the structure: 1 covalent (additive adduct).
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 P0AB87
- Elsewhere: RCSB PDB 4FUA · PDBe 4FUA · UniProt P0AB87
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