MolNFT v1 · #136817 · protein
Crystal structure of LARP1-unique domain DM15 bound to M7GTP
5V4R · La-related protein 1: “Crystal structure of LARP1-unique domain DM15 bound to M7GTP”. X-ray diffraction, 1 ligand (MGT), 2 pockets (best druggability 0.63). MolNFT v1 #136817 on GenesisL1: 3D structure, binding sites and pockets in…
- PDB
- 5V4R
- Type
- protein
- Length
- 304 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- La-related protein 1
- UniProt
- Q6PKG0
- Ligands
- MGT
- Pockets
- 2 · best druggability 0.63
Structure
x-ray diffraction · 2 distinct chains · 74% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | La-related protein 1 | protein | 152 | 74% helix, 0% strand | Q6PKG0 |
| B | La-related protein 1 | protein | 152 | 74% helix, 0% strand | Q6PKG0 |
Ligands and binding sites
- MGT · 7N-methyl-8-hydroguanosine-5'-triphosphate · ligand · chains A, B
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 | 438 | 0.63 | 0.76 | 44 | MGT |
| 2 | 123 | 0.40 | 0.75 | 25 | empty |
Interfaces
1 interface between chains.
- A–B · 1206 Ų buried · 8 hydrogen bonds · protein-protein
Compared structures
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 Q6PKG0
- Elsewhere: RCSB PDB 5V4R · PDBe 5V4R · UniProt Q6PKG0
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