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Crystal structure of the amino-terminal domain (atd) of iglur delta-1 (GLUD1)

Analyse Crystal structure of the amino-terminal domain (atd) of iglur delta-1 (GLUD1) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5KC9
Type: protein
Length: 1,158 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: Q61627
Ligands: NAG, CL

Structure

x-ray diffraction · 3 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	—	protein	404	—	Q61627
B	—	protein	382	—	Q61627
C	—	protein	372	—	Q61627

Ligands and binding sites

NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 3 copies · chains A, C, B
CL · Chloride ion · ion · 14 copies · chains A, B, C
EDO · 1,2-ethanediol · additive · 29 copies · chains A, B, C
BU1 · 1,4-butanediol · additive · 2 copies · chains A, C
PG4 · Tetraethylene glycol · additive · chains A, B

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

Compared structures

5KC9 · Crystal structure of the amino-terminal domain (ATD) of iGluR Delta-1 (GluD1) · the same entry in another collection · chain A against A, TM-score 1.00
Q61627 · AlphaFold monomer V2.0 prediction for glutamate receptor ionotropic, delta-1 (Q61627) · a predicted model of the same protein · chain B against A, TM-score 0.97

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 Q61627
Elsewhere: RCSB PDB 5KC9 · PDBe 5KC9 · UniProt Q61627

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