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Cryo-EM structure of human TMEM120A in the coash-free state

Analyse Cryo-EM structure of human TMEM120A in the coash-free state in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7F3U
Type: protein
Length: 656 residues
Chains: 2
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Transmembrane protein 120A
UniProt: Q9BXJ8
Pockets: 11 · best druggability 0.80

Structure

electron microscopy · 1 distinct chain · 80% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Transmembrane protein 120A	protein	328	80% helix, 0% strand	Q9BXJ8

Pockets

11 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1102	0.80	0.81	91	empty
2	1198	0.78	0.79	99	empty
3	515	0.72	0.81	46	empty
4	366	0.70	0.82	62	empty
5	515	0.64	0.76	33	empty

Interfaces

1 interface between chains.

A–B · 1609 Å² buried · 6 hydrogen bonds · protein-protein

Compared structures

7F3U · Cryo-EM structure of human TMEM120A in the CoASH-free state · the same entry in another collection · chain A against A, TM-score 1.00
Q9BXJ8 · AlphaFold monomer V2.0 prediction for ion channel tacan (Q9BXJ8) · a predicted model of the same protein · chain A against A, TM-score 0.85

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 Q9BXJ8
Elsewhere: RCSB PDB 7F3U · PDBe 7F3U · UniProt Q9BXJ8

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