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Cryo-EM structure of human TMEM120A

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

PDB: 7N7P
Type: protein
Length: 626 residues
Chains: 2
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Ion channel tacan
UniProt: Q9BXJ8
Ligands: COA
Pockets: 5 · best druggability 0.81

Structure

electron microscopy · 1 distinct chain · 85% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Ion channel tacan	protein	313	85% helix, 0% strand	Q9BXJ8

Ligands and binding sites

COA · Coenzyme A · ligand · 2 copies · chains A, B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

5 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	889	0.81	0.83	69	COA
2	863	0.80	0.82	67	COA
3	523	0.68	0.79	50	empty
4	485	0.66	0.77	47	empty
5	98	0.50	0.82	30	empty

Interfaces

1 interface between chains.

A–B · 3269 Å² buried · 19 hydrogen bonds · protein-protein

Compared structures

7N7P · Cryo-EM structure of human TMEM120A · 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 0.84

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 7N7P · PDBe 7N7P · UniProt Q9BXJ8

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