MolNFT v1 · #2317 · protein
GDP-fucose synthetase from escherichia COLI complex with NADPH
1BSV · Protein (GDP-fucose synthetase): “GDP-fucose synthetase from escherichia COLI complex with NADPH”. X-ray diffraction, 1 ligand (NDP), 2 pockets (best druggability 0.78). MolNFT v1 #2317 on GenesisL1: 3D structure, binding sites and…
- PDB
- 1BSV
- Type
- protein
- Length
- 317 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein (GDP-fucose synthetase)
- UniProt
- P32055
- Ligands
- NDP
- Pockets
- 2 · best druggability 0.78
Structure
x-ray diffraction · 1 distinct chain · 45% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein (GDP-fucose synthetase) | protein | 317 | 45% helix, 17% strand | P32055 |
Ligands and binding sites
- NDP · Nadph dihydro-nicotinamide-adenine-dinucleotide phosphate · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 922 | 0.78 | 0.80 | 78 | NDP |
| 2 | 55 | 0.37 | 0.79 | 15 | empty |
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 1BSV · PDBe 1BSV · UniProt P32055
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