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Structure of Orthoreovirus RNA Chaperone SigmaNS R6A mutant in complex with bile acid

Analyse Structure of Orthoreovirus RNA Chaperone SigmaNS R6A mutant in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 8TL8
Type: protein
Length: 669 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 3.2
Source: Orthoreovirus
Molecule: Protein sigma-NS
UniProt: P03526
Ligands: GCH
Pockets: 9 · best druggability 0.44

Structure

x-ray diffraction · resolution 3.2 · 2 distinct chains · 42% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Protein sigma-NS	protein	334	43% helix, 19% strand	P03526
B	Protein sigma-NS	protein	335	41% helix, 19% strand	P03526

Ligands and binding sites

GCH · Glycocholic acid · ligand · 4 copies · chains A, B

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

Pockets

9 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	163	0.44	0.75	26	empty
2	109	0.42	0.77	19	empty
3	139	0.41	0.75	22	empty
4	89	0.41	0.78	19	empty
5	62	0.36	0.78	14	empty

Interfaces

1 interface between chains.

A–B · 1019 Å² buried · 12 hydrogen bonds · protein-protein

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 P03526
Elsewhere: RCSB PDB 8TL8 · PDBe 8TL8 · UniProt P03526

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