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Structure of uridylyltransferase mutant

Analyse Structure of uridylyltransferase mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6K9Z
Type
protein
Length
610 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v2 / PDB Bank
Contract
0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner
0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution
1.78
Source
Pyrobaculum aerophilum str. IM2
Molecule
Galactose-1-phosphate uridylyltransferase
UniProt
Q8ZXN7
Ligands
UDP, ZN, FE
Pockets
6 · best druggability 0.72

Structure

x-ray diffraction · resolution 1.78 · 2 distinct chains · 31% helix, 23% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AGalactose-1-phosphate uridylyltransferaseprotein30931% helix, 23% strandQ8ZXN7
BGalactose-1-phosphate uridylyltransferaseprotein30132% helix, 23% strandQ8ZXN7

Ligands and binding sites

  • UDP · Uridine-5'-diphosphate · ligand · 2 copies · chains A, B
  • ZN · Zinc ion · metal · 4 copies · chains A, B
  • FE · Fe (III) ion · metal · 2 copies · chains A, B
  • ACT · Acetate ion · additive · chains A

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
14830.720.8241UDP
25120.690.7947UDP
34590.680.7962empty
4980.470.8122empty
5940.470.8121empty

Interfaces

1 interface between chains.

  • A–B · 3147 Ų buried · 43 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

  • 6K9Z · Structure of uridylyltransferase mutant · the same entry in another collection · chain A against A, TM-score 1.00

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