MolNFT v1 · #186890 · protein

Cryo-EM structure of a TTYH2 trans-dimer

7RTU: “Cryo-EM structure of a TTYH2 trans-dimer”. Electron microscopy, 2 ligands (NAG, BMA). MolNFT v1 #186890 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 7RTU
Type: protein
Length: 754 residues
Chains: 2
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: Q3TH73
Ligands: NAG, BMA

Structure

electron microscopy · 2 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	—	protein	395	—	Q3TH73
B	—	protein	359	—	Q3TH73

Ligands and binding sites

NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 8 copies · chains A, B
BMA · beta-D-mannopyranose · sugar · 4 copies

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

Compared structures

7RTU · Cryo-EM structure of a TTYH2 trans-dimer · the same entry in another collection · chain A against A, TM-score 1.00
Q3TH73 · AlphaFold monomer V2.0 prediction for protein tweety homolog 2 (Q3TH73) · a predicted model of the same protein · chain A against A, TM-score 0.97

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 Q3TH73
Elsewhere: RCSB PDB 7RTU · PDBe 7RTU · UniProt Q3TH73

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