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Cryo-EM structure of human TPC2 channel in the apo state

Analyse Cryo-EM structure of human TPC2 channel in the apo state in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6NQ1
Type: protein
Length: 1,242 residues
Chains: 2
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Two pore calcium channel protein 2
UniProt: Q8NHX9
Pockets: 19 · best druggability 0.86

Structure

electron microscopy · 1 distinct chain · 70% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Two pore calcium channel protein 2	protein	621	70% helix, 0% strand	Q8NHX9

Pockets

19 pockets found on a 1 Å grid, 12 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	844	0.86	0.88	49	empty
2	656	0.70	0.78	57	empty
3	206	0.68	0.85	38	empty
4	244	0.67	0.84	42	empty
5	353	0.63	0.78	29	empty

Interfaces

1 interface between chains.

A–B · 4467 Å² buried · 22 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 3 disulfide (disulfide).

Compared structures

6NQ1 · Cryo-EM structure of human TPC2 channel in the apo state · the same entry in another collection · chain A against A, TM-score 1.00
Q8NHX9 · AlphaFold monomer V2.0 prediction for two pore calcium channel protein 2 (Q8NHX9) · a predicted model of the same protein · chain A against A, TM-score 0.98

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 Q8NHX9
Elsewhere: RCSB PDB 6NQ1 · PDBe 6NQ1 · UniProt Q8NHX9

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