MolNFT v1 · #119192 · protein
Crystal structure of the cryptosporidium muris cytosolic leucyl-tRNA synthetase editing domain complex with the adduct AMP-AN6426
5FOM: “Crystal structure of the cryptosporidium muris cytosolic leucyl-tRNA synthetase editing domain complex with…”. X-ray diffraction, 2 ligands (A2H, PO4), 1 pocket (best druggability 0.73). MolNFT v1 #119192 on GenesisL1: 3D structure…
- PDB
- 5FOM
- Type
- protein
- Length
- 274 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Leucyl-tRNA synthetase
- EC
- 6.1.1.4
- UniProt
- B6AA20
- Ligands
- A2H, PO4
- Pockets
- 1 · best druggability 0.73
Structure
x-ray diffraction · 1 distinct chain · 34% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Leucyl-tRNA synthetase (EC 6.1.1.4) | protein | 274 | 34% helix, 26% strand | B6AA20 |
Ligands and binding sites
- A2H · 4-chloro-3-aminomethyl-7-[ethoxy]-3H-benzo[c][1, 2]oxaborol-1-ol modified adenosine · ligand · chains A
- PO4 · Phosphate ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 358 | 0.73 | 0.84 | 34 | A2H |
Compared structures
- 5FOM · Crystal structure of the Cryptosporidium muris cytosolic leucyl-tRNA synthetase editing… · 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 B6AA20
- Elsewhere: RCSB PDB 5FOM · PDBe 5FOM · UniProt B6AA20
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.