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Cryo-EM structure of TMEM16F in digitonin without calcium

Analyse Cryo-EM structure of TMEM16F in digitonin without calcium in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6P47
Type: protein
Length: 1,450 residues
Chains: 2
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Anoctamin-6
UniProt: Q6P9J9
Pockets: 20 · best druggability 0.79

Structure

electron microscopy · 1 distinct chain · 53% helix, 3% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Anoctamin-6	protein	725	53% helix, 3% strand	Q6P9J9

Pockets

20 pockets found on a 1 Å grid, 15 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1131	0.79	0.80	79	empty
2	1078	0.79	0.80	74	empty
3	140	0.74	0.93	27	empty
4	555	0.74	0.82	65	empty
5	1011	0.73	0.76	90	empty

Interfaces

1 interface between chains.

A–B · 994 Å² buried · 5 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 6 disulfide (disulfide).

Compared structures

6P47 · Cryo-EM structure of TMEM16F in digitonin without calcium · the same entry in another collection · chain A against A, TM-score 1.00
Q6P9J9 · AlphaFold monomer V2.0 prediction for anoctamin-6 (Q6P9J9) · a predicted model of the same protein · chain B against A, TM-score 0.91

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 Q6P9J9
Elsewhere: RCSB PDB 6P47 · PDBe 6P47 · UniProt Q6P9J9

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