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Spinosyn rhamnosyltransferase spng

Analyse Spinosyn rhamnosyltransferase spng in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3TSA
Type
protein
Length
744 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Ndp-rhamnosyltransferase
EC
2.4.1.-
UniProt
Q9ALM8
Ligands
GLC, MG
Pockets
7 · best druggability 0.79

Structure

x-ray diffraction · 2 distinct chains · 48% helix, 16% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ANdp-rhamnosyltransferase (EC 2.4.1.-)protein37248% helix, 16% strandQ9ALM8
BNdp-rhamnosyltransferase (EC 2.4.1.-)protein37248% helix, 16% strandQ9ALM8

Ligands and binding sites

  • GLC · alpha-D-glucopyranose · sugar · chains B
  • MG · Magnesium ion · metal · chains A

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
17460.790.8372empty
25790.790.8462empty
31720.690.8835empty
41530.680.8834empty
5850.440.8019empty

Interfaces

1 interface between chains.

  • A–B · 1299 Ų buried · 19 hydrogen bonds · protein-protein

Compared structures

  • 3TSA · Spinosyn Rhamnosyltransferase SpnG · the same entry in another collection · chain A against A, TM-score 1.00

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