MolNFT v1 · #184247 · protein

Lassa virus L protein with endonuclease and C-terminal domains in close proximity [mid-link]

7OJJ · RNA-directed RNA polymerase L: “Lassa virus L protein with endonuclease and C-terminal domains in close proximity [mid-link]”. Electron microscopy, 2 ligands (ZN, MG), 20 pockets (best druggability 0.78). MolNFT v1 #184247 on…

PDB: 7OJJ
Type: protein
Length: 1,785 residues
Chains: 1
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: RNA-directed RNA polymerase L
EC: 2.7.7.48, 3.1.-.-
UniProt: A0A3S8NV63
Ligands: ZN, MG
Pockets: 20 · best druggability 0.78

Structure

electron microscopy · 1 distinct chain · 46% helix, 9% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
L	RNA-directed RNA polymerase L (EC 2.7.7.48, 3.1.-.-)	protein	1785	46% helix, 9% strand	A0A3S8NV63

Ligands and binding sites

ZN · Zinc ion · metal · chains L
MG · Magnesium ion · metal · chains L

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	833	0.78	0.81	102	empty
2	164	0.77	0.93	36	empty
3	1023	0.72	0.76	80	empty
4	56	0.71	0.97	15	empty
5	59	0.70	0.96	16	empty

Compared structures

7OJJ · Lassa virus L protein with endonuclease and C-terminal domains in close proximity… · the same entry in another collection · chain L against L, 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 A0A3S8NV63
Elsewhere: RCSB PDB 7OJJ · PDBe 7OJJ · UniProt A0A3S8NV63

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