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Mnemiopsis leidyi ML032222A iglur lbd R703K mutant glycine complex

Analyse Mnemiopsis leidyi ML032222A iglur lbd R703K mutant glycine complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5CMB
Type
protein
Length
502 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
ML032222A iglur
Ligands
GLY, MG, SO4
Pockets
8 · best druggability 0.58

Structure

x-ray diffraction · 2 distinct chains · 35% helix, 26% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AML032222A iglurprotein24736% helix, 27% strand—
BML032222A iglurprotein25535% helix, 26% strand—

Ligands and binding sites

  • GLY · Glycine · ligand · 2 copies · chains A, B
  • MG · Magnesium ion · metal · chains A, B
  • SO4 · Sulfate ion · ion · chains B

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

Pockets

8 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11980.580.8035empty
21030.500.8121empty
31100.480.8019empty
4690.320.7519empty
5610.310.7614empty

Interfaces

1 interface between chains.

  • A–B · 1050 Ų buried · 18 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 3 disulfide (disulfide).

Compared structures

  • 5CMB · Mnemiopsis leidyi ML032222a iGluR LBD R703K mutant glycine complex · the same entry in another collection · chain A against A, TM-score 1.00

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