MolNFT v1 · #184120 · protein

Apo-structure of lassa virus L protein (well-resolved endonuclease) [apo-endo]

7OE3 · RNA-directed RNA polymerase L: “Apo-structure of lassa virus L protein (well-resolved endonuclease) [apo-endo]”. Electron microscopy, 2 ligands (ZN, MG), 20 pockets (best druggability 0.78). MolNFT v1 #184120 on GenesisL1: 3D…

PDB: 7OE3
Type: protein
Length: 1,478 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 · 49% 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	1478	49% 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, 11 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	701	0.78	0.82	75	empty
2	53	0.72	0.98	15	empty
3	1046	0.72	0.76	109	empty
4	589	0.71	0.79	74	empty
5	193	0.70	0.87	45	empty

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

7OE3 · Apo-structure of Lassa virus L protein (well-resolved endonuclease) [APO-ENDO] · 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 7OE3 · PDBe 7OE3 · UniProt A0A3S8NV63

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