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Cryo-EM structure of human TRPML1 with PI35P2

Analyse Cryo-EM structure of human TRPML1 with PI35P2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6E7P
Type: protein
Length: 1,900 residues
Chains: 4
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: Q9GZU1
Ligands: HZ7

Structure

electron microscopy · 1 distinct chain.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D	—	protein	475	—	Q9GZU1

Ligands and binding sites

HZ7 · (1R,2S,3S,4R,5S,6R)-5-{[(R)-[(2R)-2,3-bis{[(1s)-1-hydroxyoctyl]oxy}propoxy](hydroxy)phosphoryl]oxy}-2,4, 6-trihydroxycyclohexane-1,3-diyl bis[dihydrogen (phosphate)] · ligand · 4 copies · chains A, B, C, D

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

Compared structures

6E7P · cryo-EM structure of human TRPML1 with PI35P2 · 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 0.96

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 Q9GZU1
Elsewhere: RCSB PDB 6E7P · PDBe 6E7P · UniProt Q9GZU1

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