MolNFT v1 · #85770 · protein
Crystal structure of the glycosyltransferase snogd from streptomyces nogalater
4AMG: “Crystal structure of the glycosyltransferase snogd from streptomyces nogalater”. X-ray diffraction, 10 pockets (best druggability 0.75). MolNFT v1 #85770 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 4AMG
- Type
- protein
- Length
- 732 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Snogd
- UniProt
- Q9RN61
- Pockets
- 10 · best druggability 0.75
Structure
x-ray diffraction · 2 distinct chains · 40% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Snogd | protein | 362 | 42% helix, 15% strand | Q9RN61 |
| B | Snogd | protein | 370 | 39% helix, 15% strand | Q9RN61 |
Pockets
10 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 321 | 0.75 | 0.87 | 41 | empty |
| 2 | 335 | 0.72 | 0.85 | 41 | empty |
| 3 | 535 | 0.65 | 0.76 | 67 | empty |
| 4 | 381 | 0.64 | 0.78 | 46 | empty |
| 5 | 230 | 0.59 | 0.80 | 34 | empty |
Interfaces
1 interface between chains.
- A–B · 1506 Ų buried · 21 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 modified (methylation).
Compared structures
- 4AMG · Crystal structure of the glycosyltransferase SnogD from Streptomyces nogalater · 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 Q9RN61
- Elsewhere: RCSB PDB 4AMG · PDBe 4AMG · UniProt Q9RN61
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.