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Structure of a C-terminal domain of a reptarenavirus L protein with M7GTP

Analyse Structure of a C-terminal domain of a reptarenavirus L protein with M7GTP in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5MUY
Type: protein
Length: 654 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: L protein
UniProt: J7HBG8
Ligands: MGT
Pockets: 7 · best druggability 0.77

Structure

x-ray diffraction · 1 distinct chain · 39% helix, 25% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	L protein	protein	327	39% helix, 25% strand	J7HBG8

Ligands and binding sites

MGT · 7N-methyl-8-hydroguanosine-5'-triphosphate · ligand · chains A, B

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

Pockets

7 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1105	0.77	0.79	74	empty
2	752	0.69	0.76	76	empty
3	851	0.69	0.75	86	empty
4	97	0.51	0.83	19	MGT
5	54	0.32	0.77	16	empty

Interfaces

1 interface between chains.

A–B · 3152 Å² buried · 54 hydrogen bonds · protein-protein

Compared structures

5MUY · Structure of a C-terminal domain of a reptarenavirus L protein with m7GTP · 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 J7HBG8
Elsewhere: RCSB PDB 5MUY · PDBe 5MUY · UniProt J7HBG8

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