MolNFT v2 · #150007 · protein

Structure of the AMPAR GluA3 N-terminal domain bound to phosphate

6FPJ: “Structure of the AMPAR GluA3 N-terminal domain bound to phosphate”. X-ray diffraction at 1.96, 2 ligands (NAG, PO4). MolNFT v2 #150007 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 6FPJ
Type: protein
Length: 1,118 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 1.96
Source: Rattus norvegicus
UniProt: P19492
Ligands: NAG, PO4

Structure

x-ray diffraction · resolution 1.96 · 3 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	—	protein	374	—	P19492
B	—	protein	379	—	P19492
C	—	protein	365	—	P19492

Ligands and binding sites

NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 8 copies · chains A, B, C
PO4 · Phosphate ion · ion · 7 copies · chains A, B, C
DMS · Dimethyl sulfoxide · additive · 7 copies · chains A, B, C
GOL · Glycerol · additive · chains B

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

Compared structures

6FPJ · Structure of the ampar GLUA3 N-terminal domain bound to phosphate · 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 C 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 P19492
Elsewhere: RCSB PDB 6FPJ · PDBe 6FPJ · UniProt P19492

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