Research workbench

Dnqx-bound GLUK2-2XNETO2 complex

Analyse Dnqx-bound GLUK2-2XNETO2 complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7F5A
Type: protein
Length: 3,912 residues
Chains: 6
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: P42260, C6K2K4
Ligands: NAG, BMA

Structure

electron microscopy · 4 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, C	—	protein	835	—	P42260
B, D	—	protein	818	—	P42260
E	—	protein	309	—	C6K2K4
F	—	protein	297	—	C6K2K4

Ligands and binding sites

NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 18 copies · chains A, B, C, D
BMA · beta-D-mannopyranose · sugar · 4 copies · chains A, B, C, D

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

Compared structures

7F5A · DNQX-bound GluK2-2xNeto2 complex · the same entry in another collection · chain F against F, TM-score 1.00
P42260 · AlphaFold monomer V2.0 prediction for glutamate receptor ionotropic, kainate 2 (P42260) · a predicted model of the same protein · chain C against A, TM-score 0.70
C6K2K4 · AlphaFold monomer V2.0 prediction for neuropilin and tolloid-like protein 2 (C6K2K4) · a predicted model of the same protein · chain E against A, TM-score 0.68

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 P42260
Every structure of UniProt C6K2K4
Elsewhere: RCSB PDB 7F5A · PDBe 7F5A · UniProt P42260 · UniProt C6K2K4

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