MolNFT v1 · #107530 · protein
X-ray structure and activities of an essential mononegavirales L- protein domain
4UCZ · RNA-directed RNA polymerase L: “X-ray structure and activities of an essential mononegavirales L- protein domain”. X-ray diffraction, 3 ligands (GTP, GMP, ZN), 7 pockets (best druggability 0.63). MolNFT v1 #107530 on GenesisL1: 3D…
- PDB
- 4UCZ
- Type
- protein
- Length
- 756 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- RNA-directed RNA polymerase L
- UniProt
- Q91L20
- Ligands
- GTP, GMP, ZN
- Pockets
- 7 · best druggability 0.63
Structure
x-ray diffraction · 2 distinct chains · 43% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | RNA-directed RNA polymerase L | protein | 381 | 43% helix, 13% strand | Q91L20 |
| B | RNA-directed RNA polymerase L | protein | 375 | 43% helix, 13% strand | Q91L20 |
Ligands and binding sites
- GTP · Guanosine-5'-triphosphate · ligand · chains A
- GMP · Guanosine · ligand · chains B
- ZN · Zinc ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 461 | 0.63 | 0.77 | 48 | GTP |
| 2 | 533 | 0.62 | 0.75 | 48 | empty |
| 3 | 442 | 0.61 | 0.76 | 47 | GMP |
| 4 | 246 | 0.53 | 0.76 | 35 | empty |
| 5 | 53 | 0.38 | 0.81 | 12 | empty |
Interfaces
1 interface between chains.
- A–B · 771 Ų buried · 14 hydrogen bonds · protein-protein
Compared structures
- 4UCZ · X-ray structure and activities of an essential Mo gavirales L- protein domain · 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 Q91L20
- Elsewhere: RCSB PDB 4UCZ · PDBe 4UCZ · UniProt Q91L20
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