Research workbench

Structure of mechanically activated ion channel OSCA1.2 in lmng

Analyse Structure of mechanically activated ion channel OSCA1.2 in lmng in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6MGW
Type: protein
Length: 1,268 residues
Chains: 2
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Calcium permeable stress-gated cation channel 1
UniProt: Q5XEZ5
Pockets: 17 · best druggability 0.75

Structure

electron microscopy · 1 distinct chain · 69% helix, 4% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Calcium permeable stress-gated cation channel 1	protein	634	69% helix, 4% strand	Q5XEZ5

Pockets

17 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	749	0.75	0.80	72	empty
2	472	0.75	0.83	44	empty
3	452	0.62	0.76	49	empty
4	417	0.60	0.75	40	empty
5	99	0.45	0.80	17	empty

Interfaces

1 interface between chains.

A–B · 1372 Å² buried · 16 hydrogen bonds · protein-protein

Compared structures

6MGW · Structure of mechanically activated ion channel OSCA1.2 in LMNG · 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 A against A, TM-score 0.93

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 6MGW · PDBe 6MGW · UniProt Q5XEZ5

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.