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Structural basis for conductance through TRIC cation channels

Analyse Structural basis for conductance through TRIC cation channels in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5WUC
Type: protein
Length: 194 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 1.6
Source: Sulfolobus acidocaldarius
Molecule: Uncharacterized protein
UniProt: A0A0U3H1E6
Ligands: NA
Pockets: 1 · best druggability 0.53

Structure

x-ray diffraction · resolution 1.6 · 1 distinct chain · 79% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Uncharacterized protein	protein	194	79% helix, 0% strand	A0A0U3H1E6

Ligands and binding sites

NA · Sodium ion · metal · 2 copies · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	73	0.53	0.85	20	empty

Compared structures

5WUC · Structural basis for conductance through tric cation channels · 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 A0A0U3H1E6
Elsewhere: RCSB PDB 5WUC · PDBe 5WUC · UniProt A0A0U3H1E6

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