MolNFT v1 · #107515 · protein
X-ray structure and activities of an essential mononegavirales L- protein domain
4UCK · RNA-directed RNA polymerase L: “X-ray structure and activities of an essential mononegavirales L- protein domain”. X-ray diffraction, 2 ligands (SAM, ZN), 5 pockets (best druggability 0.65). MolNFT v1 #107515 on GenesisL1: 3D…
- PDB
- 4UCK
- Type
- protein
- Length
- 746 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- RNA-directed RNA polymerase L
- UniProt
- Q91L20
- Ligands
- SAM, ZN
- Pockets
- 5 · best druggability 0.65
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 | 370 | 44% helix, 13% strand | Q91L20 |
| B | RNA-directed RNA polymerase L | protein | 376 | 43% helix, 13% strand | Q91L20 |
Ligands and binding sites
- SAM · S-adenosylmethionine · ligand · 2 copies · chains A, 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
5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 570 | 0.65 | 0.76 | 66 | SAM |
| 2 | 592 | 0.65 | 0.76 | 51 | empty |
| 3 | 298 | 0.53 | 0.75 | 48 | SAM |
| 4 | 60 | 0.38 | 0.80 | 14 | empty |
| 5 | 61 | 0.28 | 0.73 | 19 | empty |
Interfaces
1 interface between chains.
- A–B · 810 Ų buried · 15 hydrogen bonds · protein-protein
Compared structures
- 4UCK · 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 4UCK · PDBe 4UCK · UniProt Q91L20
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