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Crystal structure of the GLUA2O lbd in complex with glutamate and LY451395

Analyse Crystal structure of the GLUA2O lbd in complex with glutamate and LY451395 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5YBG
Type: protein
Length: 1,566 residues
Chains: 6
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: P42262
Ligands: 8SO, ZN

Structure

x-ray diffraction · 3 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, D, F	—	protein	261	—	P42262
C	—	protein	260	—	P42262
E	—	protein	262	—	P42262

Ligands and binding sites

8SO · N-[(2R)-2-[4-[4-[2-(methylsulfonylamino) ethyl]phenyl]phenyl]propyl]propane-2-sulfonamide · ligand · 3 copies · chains A, B, C, D, E, F
ZN · Zinc ion · metal · 10 copies · chains A, C, B, D, E, F
ACT · Acetate ion · additive · 5 copies · chains A, C, D, E
GOL · Glycerol · additive · 2 copies · chains A, B, E, F

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

Compared structures

5YBG · Crystal structure of the GluA2o LBD in complex with glutamate and LY451395 · the same entry in another collection · chain E against E, TM-score 1.00
P42262 · AlphaFold monomer V2.0 prediction for glutamate receptor 2 (P42262) · a predicted model of the same protein · chain E 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 P42262
Elsewhere: RCSB PDB 5YBG · PDBe 5YBG · UniProt P42262

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