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Human ogt in complex with udp and fused substrate peptide (TAB1)

Analyse Human ogt in complex with udp and fused substrate peptide (TAB1) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5LVV
Type
protein
Length
720 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Udp-N-acetylglucosamine--peptide N- acetylglucosaminyltransferase 110 kda SUBUNIT,UDP-N…
EC
2.4.1.255
UniProt
O15294
Ligands
UDP, NAG
Pockets
5 · best druggability 0.80

Structure

x-ray diffraction · 1 distinct chain · 50% helix, 12% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AUdp-N-acetylglucosamine--peptide N- acetylglucosaminyltransferase 110 kda SUBUNIT,UDP-N- acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kda subunit (EC 2.4.1.255)protein72050% helix, 12% strandO15294

Ligands and binding sites

  • UDP · Uridine-5'-diphosphate · ligand · chains A
  • NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 3 copies · chains A

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
111310.800.8299NAG
23010.800.9154UDP, NAG
3540.700.9716empty
42860.600.7933empty
51050.360.7420empty

Modifications

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

Compared structures

  • 5LVV · Human OGT in complex with UDP and fused substrate peptide (Tab1) · the same entry in another collection · chain A against A, TM-score 1.00
  • O15294 · AlphaFold monomer V2.0 prediction for udp-N-acetylglucosamine-- peptide… · a predicted model of the same protein · chain A against A, TM-score 0.94

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