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Crystal structure of the BETA3 subunit extracellular domain of nicotinic acetylcholine receptor

Analyse Crystal structure of the BETA3 subunit extracellular domain of nicotinic… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 8A5U
Type: protein
Length: 201 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Neuronal acetylcholine receptor subunit beta-3
UniProt: Q05901
Ligands: BCN, NAG

Structure

x-ray diffraction · 1 distinct chain · 7% helix, 49% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
B	Neuronal acetylcholine receptor subunit beta-3	protein	201	7% helix, 49% strand	Q05901

Ligands and binding sites

BCN · Bicine · ligand · chains B
NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 2 copies · chains B
EDO · 1,2-ethanediol · additive · chains B

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

Modifications

Observed in the structure: 2 glycan, 1 disulfide (N-glycosylation, disulfide).

Compared structures

8A5U · Crystal structure of the beta3 subunit extracellular domain of nicotinic acetylcholine… · the same entry in another collection · chain B against B, TM-score 1.00
Q05901 · AlphaFold monomer V2.0 prediction for neuronal acetylcholine receptor subunit beta-3… · a predicted model of the same protein · chain B against A, TM-score 0.95

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 Q05901
Elsewhere: RCSB PDB 8A5U · PDBe 8A5U · UniProt Q05901

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