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Glge isoform 1 from streptomyces coelicolor D394A mutant co- crystallised with maltodextrin

Analyse Glge isoform 1 from streptomyces coelicolor D394A mutant co- crystallised with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5LGW
Type
protein
Length
1,296 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Alpha-1,4-GLUCAN:MALTOSE-1-phosphate maltosyltransferase 1
EC
2.4.99.16
UniProt
Q9L1K2
Ligands
GLC, BGC
Pockets
13 · best druggability 0.77

Structure

x-ray diffraction · 1 distinct chain · 35% helix, 25% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BAlpha-1,4-GLUCAN:MALTOSE-1-phosphate maltosyltransferase 1 (EC 2.4.99.16)protein64835% helix, 25% strandQ9L1K2

Ligands and binding sites

  • GLC · alpha-D-glucopyranose · sugar · 27 copies · chains B, A
  • BGC · beta-D-glucopyranose · sugar · 2 copies · chains A, B
  • EDO · 1,2-ethanediol · additive · 4 copies · chains A, B
  • CIT · Citric acid · additive · chains A

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

Pockets

13 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
18290.770.8054EDO
210650.760.79116empty
38180.760.8054EDO
42650.680.8432BGC, GLC, EDO
52760.680.8334BGC, GLC, EDO

Interfaces

1 interface between chains.

  • A–B · 2285 Ų buried · 33 hydrogen bonds · protein-protein

Compared structures

  • 5LGW · GlgE isoform 1 from Streptomyces coelicolor D394A mutant co-crystallised with maltodextrin · the same entry in another collection · chain A against A, TM-score 1.00
  • Q9L1K2 · AlphaFold monomer V2.0 prediction for alpha-1,4-GLUCAN:MALTOSE-1-phosphate… · a predicted model of the same protein · chain A against A, TM-score 1.00

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