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High-resolution structure of the N-terminal endonuclease domain of the lassa virus L polymerase
Analyse High-resolution structure of the N-terminal endonuclease domain of the lassa… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4MIW
- Type
- protein
- Length
- 170 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- RNA-directed RNA polymerase L
- EC
- 2.7.7.48
- UniProt
- Q6GWS2
- Ligands
- MG
Structure
x-ray diffraction · 1 distinct chain · 53% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | RNA-directed RNA polymerase L (EC 2.7.7.48) | protein | 170 | 53% helix, 15% strand | Q6GWS2 |
Ligands and binding sites
- MG · Magnesium ion · metal · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 4MIW · High-resolution structure of the N-terminal endonuclease domain of the Lassa virus L… · 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 Q6GWS2
- Elsewhere: RCSB PDB 4MIW · PDBe 4MIW · UniProt Q6GWS2
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