MolNFT v1 · #116041 · protein
Crystal structure of the 16S rRNA (ADENINE(1408)-N(1))- methyltransferase with its reaction by-product sah from catenulisporales acidiphilia
5D1N · Uncharacterized protein: “Crystal structure of the 16S rRNA (ADENINE(1408)-N(1))- methyltransferase with its reaction by-product sah…”. X-ray diffraction, 1 ligand (SAH), 2 pockets (best druggability 0.52). MolNFT v1 #116041 on…
- PDB
- 5D1N
- Type
- protein
- Length
- 222 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Uncharacterized protein
- UniProt
- C7Q5P8
- Ligands
- SAH
- Pockets
- 2 · best druggability 0.52
Structure
x-ray diffraction · 1 distinct chain · 34% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Uncharacterized protein | protein | 222 | 34% helix, 27% strand | C7Q5P8 |
Ligands and binding sites
- SAH · S-adenosyl-L-homocysteine · 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 | 159 | 0.52 | 0.79 | 30 | SAH |
| 2 | 94 | 0.36 | 0.75 | 18 | empty |
Compared structures
- 5D1N · Crystal structure of the 16S rRNA (adenine(1408)-N(1))-methyltransferase with its… · 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 C7Q5P8
- Elsewhere: RCSB PDB 5D1N · PDBe 5D1N · UniProt C7Q5P8
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.