Research workbench

Cryo-EM structure of mouse apo TRPML1 channel at 2.598 ångström resolution

Analyse Cryo-EM structure of mouse apo TRPML1 channel at 2.598 ångström resolution in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7SQ8
Type: protein
Length: 1,852 residues
Chains: 4
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: Q99J21
Ligands: NAG, NA

Structure

electron microscopy · 1 distinct chain.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D	—	protein	463	—	Q99J21

Ligands and binding sites

NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 8 copies · chains A, B, C, D
NA · Sodium ion · metal · chains A, B, C, D

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

Compared structures

7SQ8 · Cryo-EM structure of mouse apo TRPML1 channel at 2.598 Angstrom resolution · the same entry in another collection · chain A against A, TM-score 1.00
Q99J21 · AlphaFold monomer V2.0 prediction for mucolipin-1 (Q99J21) · 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 Q99J21
Elsewhere: RCSB PDB 7SQ8 · PDBe 7SQ8 · UniProt Q99J21

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