MolNFT v1 · #147216 · protein
Crystal structure of bacterial N-acetylglucosamine transferase nleb
6E66: “Crystal structure of bacterial N-acetylglucosamine transferase nleb”. X-ray diffraction, 2 pockets (best druggability 0.38). MolNFT v1 #147216 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6E66
- Type
- protein
- Length
- 279 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Nleb
- UniProt
- A0A2D0NUY1
- Pockets
- 2 · best druggability 0.38
Structure
x-ray diffraction · 1 distinct chain · 42% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Nleb | protein | 279 | 42% helix, 17% strand | A0A2D0NUY1 |
Ligands and binding sites
- EDO · 1,2-ethanediol · additive · 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, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 111 | 0.38 | 0.75 | 24 | empty |
| 2 | 57 | 0.38 | 0.80 | 13 | empty |
Modifications
Observed in the structure: 6 modified (artifact, engineered).
Compared structures
- 6E66 · Crystal structure of bacterial N-acetylglucosamine transferase NleB · 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 A0A2D0NUY1
- Elsewhere: RCSB PDB 6E66 · PDBe 6E66 · UniProt A0A2D0NUY1
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