Research workbench

Glic-gabaar ALPHA1 chimera crystallized at PH4.6

Analyse Glic-gabaar ALPHA1 chimera crystallized at PH4.6 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5OSA
Type: protein
Length: 1,565 residues
Chains: 5
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: Q7NDN8, P62812
Ligands: D12, Y01, CL

Structure

x-ray diffraction · 1 distinct chain.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D, E	—	protein	313	—	Q7NDN8, P62812

Ligands and binding sites

D12 · Dodecane · ligand · 8 copies · chains A, B, C, D, E
Y01 · Cholesterol hemisuccinate · ligand · 5 copies · chains A, E, B, C, D
CL · Chloride ion · ion · 7 copies · chains A, B, C, D, E
ACT · Acetate ion · additive · 8 copies · chains A, E, B, C, D

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

Compared structures

5OSA · GLIC-GABAAR alpha1 chimera crystallized at pH4.6 · the same entry in another collection · chain E against E, TM-score 1.00
Q7NDN8 · AlphaFold monomer V2.0 prediction for proton-gated ion channel (Q7NDN8) · a predicted model of the same protein · chain D against A, TM-score 0.95
P62812 · AlphaFold monomer V2.0 prediction for gamma-aminobutyric acid receptor subunit alpha-1… · a predicted model of the same protein · chain D against A, TM-score 0.91

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 Q7NDN8
Every structure of UniProt P62812
Elsewhere: RCSB PDB 5OSA · PDBe 5OSA · UniProt Q7NDN8 · UniProt P62812

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