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Crystal structure of a glycosyltransferase involved in the glycosylation of the major capsid of pbcv-1

Analyse Crystal structure of a glycosyltransferase involved in the glycosylation of the… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2P72
Type
protein
Length
403 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Putative glycosyltransferase (mannosyltransferase) involved in glycosylating the pbcv-1…
UniProt
Q89399
Ligands
UPG, MN
Pockets
3 · best druggability 0.62

Structure

x-ray diffraction · 2 distinct chains · 37% helix, 19% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
APutative glycosyltransferase (mannosyltransferase) involved in glycosylating the pbcv-1 major capsid proteinprotein19938% helix, 20% strandQ89399
BPutative glycosyltransferase (mannosyltransferase) involved in glycosylating the pbcv-1 major capsid proteinprotein20437% helix, 17% strandQ89399

Ligands and binding sites

  • UPG · Uridine-5'-diphosphate-glucose · ligand · chains B
  • MN · Manganese (II) ion · metal · 2 copies · chains A, B

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12500.620.8131UPG
23660.600.7733MN
33010.520.7438empty

Interfaces

1 interface between chains.

  • A–B · 148 Ų buried · 0 hydrogen bonds · protein-protein

Compared structures

  • 2P72 · crystal structure of a glycosyltransferase involved in the glycosylation of the major… · the same entry in another collection · chain A against A, TM-score 1.00

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