MolNFT v1 · #118922 · protein
Integral membrane protein lipooligosaccharide phosphoethanolamine transferase a (epta) from neisseria meningitidis
5FGN: “Integral membrane protein lipooligosaccharide phosphoethanolamine transferase a (epta) from neisseria…”. X-ray diffraction, 2 ligands (BGL, ZN), 6 pockets (best druggability 0.72). MolNFT v1 #118922 on GenesisL1: 3D structure…
- PDB
- 5FGN
- Type
- protein
- Length
- 536 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Lipooligosaccharide phosphoethanolamine transferase a
- UniProt
- E3D1H8
- Ligands
- BGL, ZN
- Pockets
- 6 · best druggability 0.72
Structure
x-ray diffraction · 1 distinct chain · 51% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Lipooligosaccharide phosphoethanolamine transferase a | protein | 536 | 51% helix, 12% strand | E3D1H8 |
Ligands and binding sites
- BGL · 2-O-octyl-beta-D-glucopyranose · ligand · chains A
- ZN · Zinc ion · metal · chains A
- LMT · Dodecyl-beta-D-maltoside · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 293 | 0.72 | 0.85 | 31 | LMT |
| 2 | 215 | 0.50 | 0.76 | 34 | empty |
| 3 | 173 | 0.48 | 0.76 | 25 | empty |
| 4 | 68 | 0.33 | 0.76 | 20 | empty |
| 5 | 64 | 0.28 | 0.73 | 19 | empty |
Modifications
Observed in the structure: 5 disulfide (disulfide).
Compared structures
- 5FGN · Integral membrane protein lipooligosaccharide phosphoethanolamine transferase A (EptA)… · 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
- Every structure of UniProt E3D1H8
- Elsewhere: RCSB PDB 5FGN · PDBe 5FGN · UniProt E3D1H8
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.