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Apo-structure of lassa virus L protein (well-resolved polymerase core) [apo-core]

Analyse Apo-structure of lassa virus L protein (well-resolved polymerase core)… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7OCH
Type: protein
Length: 1,181 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 0.72

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	1181	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, 7 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	55	0.72	0.98	13	empty
2	959	0.69	0.74	66	empty
3	326	0.64	0.79	29	empty
4	159	0.63	0.85	29	empty
5	546	0.60	0.74	52	empty

Compared structures

7OCH · Apo-structure of Lassa virus L protein (well-resolved polymerase core) [APO-CORE] · 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 7OCH · PDBe 7OCH · UniProt A0A3S8NV63

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