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Structure of a plant cation channel

Analyse Structure of a plant cation channel in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6IJZ
Type: protein
Length: 1,366 residues
Chains: 2
Method: electron microscopy
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 3.68
Source: Arabidopsis thaliana
Molecule: Calcium permeable stress-gated cation channel 1
UniProt: Q5XEZ5
Pockets: 14 · best druggability 0.69

Structure

electron microscopy · resolution 3.68 · 1 distinct chain · 60% helix, 2% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Calcium permeable stress-gated cation channel 1	protein	683	60% helix, 2% strand	Q5XEZ5

Pockets

14 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	631	0.69	0.77	66	empty
2	180	0.68	0.87	31	empty
3	551	0.67	0.78	57	empty
4	175	0.66	0.86	34	empty
5	503	0.65	0.77	47	empty

Interfaces

1 interface between chains.

A–B · 1338 Å² buried · 14 hydrogen bonds · protein-protein

Compared structures

6IJZ · Structure of a plant cation channel · the same entry in another collection · chain A against A, TM-score 1.00
Q5XEZ5 · AlphaFold monomer V2.0 prediction for calcium permeable stress-gated cation channel 1… · a predicted model of the same protein · chain B against A, TM-score 0.92

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 Q5XEZ5
Elsewhere: RCSB PDB 6IJZ · PDBe 6IJZ · UniProt Q5XEZ5

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