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Cryo-EM structure of GMALMT12/QUAC1 anion channel

Analyse Cryo-EM structure of GMALMT12/QUAC1 anion channel in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7W6K
Type
protein
Length
820 residues
Chains
2
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
GMALMT12/QUAC1
UniProt
I1J9K0
Pockets
9 · best druggability 0.80

Structure

electron microscopy · 1 distinct chain · 74% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BGMALMT12/QUAC1protein41074% helix, 0% strandI1J9K0

Pockets

9 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
111450.800.8199empty
24930.760.8474empty
35940.730.8063empty
4940.510.8323empty
5540.360.7913empty

Interfaces

1 interface between chains.

  • A–B · 4068 Ų buried · 19 hydrogen bonds · protein-protein

Compared structures

  • 7W6K · Cryo-EM structure of GmALMT12/QUAC1 anion channel · the same entry in another collection · chain A against A, TM-score 1.00

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