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Crystal structure of sdgb (udp, nag, and O-glycosylated sd peptide- binding form)

Analyse Crystal structure of sdgb (udp, nag, and O-glycosylated sd peptide- binding… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7VFL
Type
protein
Length
1,014 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Glycosyl transferase, group 1 family protein; Ser-asp-ser-asp-ser-asp-ser-asp
UniProt
A0A0H2XGN0
Ligands
UDP, NAG
Pockets
10 · best druggability 0.78

Structure

x-ray diffraction · 3 distinct chains · 33% helix, 26% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, CGlycosyl transferase, group 1 family proteinprotein50033% helix, 27% strandA0A0H2XGN0
DSer-asp-ser-asp-ser-asp-ser-aspprotein863% helix, 0% strand—
GSer-asp-ser-asp-ser-asp-ser-aspprotein60% helix, 0% strand—

Ligands and binding sites

  • UDP · Uridine-5'-diphosphate · ligand · 2 copies · chains A, C
  • NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 5 copies · chains A, C, D, G

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

Pockets

10 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
17080.780.8366UDP, NAG
27520.760.8166UDP, NAG
38620.750.7888empty
41010.470.8020empty
5920.430.7924empty

Interfaces

3 interfaces between chains.

  • A–C · 1412 Ų buried · 28 hydrogen bonds · protein-protein
  • A–D · 308 Ų buried · 13 hydrogen bonds · protein-protein
  • C–G · 308 Ų buried · 14 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 3 glycan (O-glycosylation).

Compared structures

  • 7VFL · Crystal structure of SdgB (UDP, NAG, and O-glycosylated SD peptide-binding form) · the same entry in another collection · chain G against G, TM-score 1.00

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