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Crystal structure of Thermoplasmatales archaeon heliorhodopsin

Analyse Crystal structure of Thermoplasmatales archaeon heliorhodopsin in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6IS6
Type: protein
Length: 250 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 2.4
Source: Thermoplasmatales archaeon SG8-52-1
Molecule: heliorhodopsin
UniProt: A0A151EDA9
Ligands: RET
Pockets: 1 · best druggability 0.75

Structure

x-ray diffraction · resolution 2.4 · 1 distinct chain · 73% helix, 8% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	heliorhodopsin	protein	250	73% helix, 8% strand	A0A151EDA9

Ligands and binding sites

RET · Retinal · ligand · chains A
OLC · (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate · additive · 14 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	191	0.75	0.90	29	OLC, RET

Modifications

Observed in the structure: 1 cofactor (retinal Schiff base).

Compared structures

6IS6 · Crystal structure of thermoplasmatales archaeon heliorhodopsin · 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 A0A151EDA9
Elsewhere: RCSB PDB 6IS6 · PDBe 6IS6 · UniProt A0A151EDA9

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