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The glic pentameric ligand-gated ion channel mutant Q193C+MMTS

Analyse The glic pentameric ligand-gated ion channel mutant Q193C+MMTS in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6HYR
Type: protein
Length: 1,555 residues
Chains: 5
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Proton-gated ion channel
UniProt: Q7NDN8
Pockets: 20 · best druggability 0.81

Structure

x-ray diffraction · 1 distinct chain · 36% helix, 33% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D, E	Proton-gated ion channel	protein	311	36% helix, 33% strand	Q7NDN8

Ligands and binding sites

LMT · Dodecyl-beta-D-maltoside · additive · chains A, B, C, D, E

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

Pockets

20 pockets found on a 1 Å grid, 15 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	503	0.81	0.88	56	LMT
2	1110	0.81	0.82	103	empty
3	703	0.79	0.83	58	empty
4	130	0.79	0.97	25	empty
5	119	0.77	0.96	24	empty

Interfaces

5 interfaces between chains.

B–C · 2366 Å² buried · 21 hydrogen bonds · protein-protein
D–E · 2359 Å² buried · 24 hydrogen bonds · protein-protein
A–B · 2337 Å² buried · 20 hydrogen bonds · protein-protein
A–E · 2287 Å² buried · 18 hydrogen bonds · protein-protein
C–D · 2252 Å² buried · 17 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 5 modified (methylation).

Compared structures

6HYR · The glic pentameric ligand-gated ion channel mutant Q193C+MMTS · 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 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 Q7NDN8
Elsewhere: RCSB PDB 6HYR · PDBe 6HYR · UniProt Q7NDN8

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