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MolNFT v1 · #182268 · protein

Cryo-EM reveals partially and fully assembled native glycine RECEPTORS,HOMOMERIC tetramer

7MLV: “Cryo-EM reveals partially and fully assembled native glycine RECEPTORS,HOMOMERIC tetramer”. Electron microscopy, 3 ligands (MAN, NAG, BMA). MolNFT v1 #182268 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB
7MLV
Type
protein
Length
1,919 residues
Chains
12
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt
F1RQB7
Ligands
MAN, NAG, BMA

Structure

electron microscopy · 8 distinct chains.

ChainMoleculeTypeResiduesSecondary structureUniProt
J—protein101——
G, F, L, H—protein115——
K—protein102——
M, I—protein103——
D—protein170—F1RQB7
A—protein310—F1RQB7
B—protein296—F1RQB7
C—protein274—F1RQB7

Ligands and binding sites

  • MAN · alpha-D-mannopyranose · sugar · 10 copies
  • NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 8 copies · chains A, B, C, D
  • BMA · beta-D-mannopyranose · sugar · 4 copies

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

Compared structures

  • 7MLV · Cryo-EM reveals partially and fully assembled native glycine receptors,homomeric tetramer · the same entry in another collection · chain J against J, TM-score 1.00

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