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Cryoem structure of full length mouse TRPML2

Analyse Cryoem structure of full length mouse TRPML2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7DYS
Type: protein
Length: 1,548 residues
Chains: 4
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Mucolipin-2
UniProt: Q8K595
Pockets: 20 · best druggability 0.87

Structure

electron microscopy · 1 distinct chain · 60% helix, 12% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D	Mucolipin-2	protein	387	60% helix, 12% strand	Q8K595

Pockets

20 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	1101	0.87	0.87	115	empty
2	421	0.69	0.80	38	empty
3	200	0.68	0.85	27	empty
4	400	0.68	0.80	39	empty
5	397	0.67	0.80	43	empty

Interfaces

6 interfaces between chains.

B–C · 2545 Å² buried · 12 hydrogen bonds · protein-protein
C–D · 2511 Å² buried · 9 hydrogen bonds · protein-protein
A–D · 2502 Å² buried · 9 hydrogen bonds · protein-protein
A–B · 2485 Å² buried · 7 hydrogen bonds · protein-protein
B–D · 21 Å² buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 8 disulfide (disulfide).

Compared structures

7DYS · CryoEM structure of full length mouse TRPML2 · the same entry in another collection · chain A against A, TM-score 1.00
Q8K595 · AlphaFold monomer V2.0 prediction for mucolipin-2 (Q8K595) · a predicted model of the same protein · chain A against A, TM-score 0.96

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 Q8K595
Elsewhere: RCSB PDB 7DYS · PDBe 7DYS · UniProt Q8K595

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