MolNFT v1 · #61442 · protein

Crystal structure of the binding domain of the AMPA subunit GLUR3 bound to glutamate

3DLN · Glutamate receptor 3: “Crystal structure of the binding domain of the AMPA subunit GLUR3 bound to glutamate”. X-ray diffraction, 2 ligands (GLU, ZN), 2 pockets (best druggability 0.43). MolNFT v1 #61442 on GenesisL1: 3D structure…

PDB: 3DLN
Type: protein
Length: 258 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Glutamate receptor 3
UniProt: P19492
Ligands: GLU, ZN
Pockets: 2 · best druggability 0.43

Structure

x-ray diffraction · 1 distinct chain · 38% helix, 22% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Glutamate receptor 3	protein	258	38% helix, 22% strand	P19492

Ligands and binding sites

GLU · Glutamic acid · ligand · chains A
ZN · Zinc ion · metal · chains A

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

Pockets

2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	141	0.43	0.75	26	empty
2	91	0.40	0.77	25	empty

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

3DLN · Crystal structure of the binding domain of the AMPA subunit GluR3 bound to glutamate · the same entry in another collection · chain A against A, TM-score 1.00
P19492 · AlphaFold monomer V2.0 prediction for glutamate receptor 3 (P19492) · 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 P19492
Elsewhere: RCSB PDB 3DLN · PDBe 3DLN · UniProt P19492

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