MolNFT v1 · #5068 · protein
GDP 4-keto-6-deoxy-D-mannose epimerase reductase
1E6U · GDP-fucose synthetase: “GDP 4-keto-6-deoxy-D-mannose epimerase reductase”. X-ray diffraction, 3 ligands (NAP, UVW, SO4), 1 pocket (best druggability 0.78). MolNFT v1 #5068 on GenesisL1: 3D structure, binding sites and pockets in…
- PDB
- 1E6U
- Type
- protein
- Length
- 315 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- GDP-fucose synthetase
- EC
- 5.1.3.-
- UniProt
- P32055
- Ligands
- NAP, UVW, SO4
- Pockets
- 1 · best druggability 0.78
Structure
x-ray diffraction · 1 distinct chain · 45% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | GDP-fucose synthetase (EC 5.1.3.-) | protein | 315 | 45% helix, 17% strand | P32055 |
Ligands and binding sites
- NAP · Nadp nicotinamide-adenine-dinucleotide phosphate · ligand · chains A
- UVW · Acetylphosphate · ligand · chains A
- SO4 · Sulfate ion · ion · 4 copies · chains A
- TRS · 2-amino-2-hydroxymethyl-propane-1,3-diol · 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 | 966 | 0.78 | 0.80 | 81 | NAP, UVW |
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 P32055
- Elsewhere: RCSB PDB 1E6U · PDBe 1E6U · UniProt P32055
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