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Human TRPML1 channel structure in closed conformation

Analyse Human TRPML1 channel structure in closed conformation in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5WJ5
Type: protein
Length: 1,828 residues
Chains: 4
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Mucolipin-1
UniProt: Q9GZU1
Pockets: 20 · best druggability 0.84

Structure

electron microscopy · 1 distinct chain · 55% helix, 12% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D	Mucolipin-1	protein	457	55% helix, 12% strand	Q9GZU1

Pockets

20 pockets found on a 1 Å grid, 14 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	216	0.84	0.96	32	empty
2	1182	0.75	0.78	85	empty
3	1182	0.75	0.78	97	empty
4	706	0.75	0.80	71	empty
5	493	0.73	0.82	31	empty

Interfaces

6 interfaces between chains.

A–D · 3725 Å² buried · 28 hydrogen bonds · protein-protein
C–D · 3718 Å² buried · 28 hydrogen bonds · protein-protein
A–B · 3717 Å² buried · 28 hydrogen bonds · protein-protein
B–C · 3700 Å² buried · 28 hydrogen bonds · protein-protein
A–C · 42 Å² buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 8 disulfide (disulfide).

Compared structures

5WJ5 · Human TRPML1 channel structure in closed conformation · the same entry in another collection · chain A against A, TM-score 1.00
Q9GZU1 · AlphaFold monomer V2.0 prediction for mucolipin-1 (Q9GZU1) · a predicted model of the same protein · chain A against A, TM-score 0.95

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 Q9GZU1
Elsewhere: RCSB PDB 5WJ5 · PDBe 5WJ5 · UniProt Q9GZU1

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