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Udp-glucose pyrophosphorylase from acinetobacter baumanii

Analyse Udp-glucose pyrophosphorylase from acinetobacter baumanii in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6IKZ
Type
protein
Length
575 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
UTP--glucose-1-phosphate uridylyltransferase
EC
2.7.7.9
UniProt
X2KZJ9
Ligands
PPV, UTP, SO4
Pockets
7 · best druggability 0.70

Structure

x-ray diffraction · 2 distinct chains · 34% helix, 22% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AUTP--glucose-1-phosphate uridylyltransferase (EC 2.7.7.9)protein29034% helix, 23% strandX2KZJ9
BUTP--glucose-1-phosphate uridylyltransferase (EC 2.7.7.9)protein28534% helix, 22% strandX2KZJ9

Ligands and binding sites

  • PPV · Pyrophosphate · ligand · chains A
  • UTP · Uridine 5'-triphosphate · ligand · chains A, B
  • SO4 · Sulfate ion · ion · 6 copies · chains A, B
  • GOL · Glycerol · additive · 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, 3 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
17770.700.7659PPV, GOL
26650.680.7662UTP, SO4
32370.580.7941empty
41450.470.7821empty
51390.460.7719empty

Interfaces

1 interface between chains.

  • A–B · 2348 Ų buried · 18 hydrogen bonds · protein-protein

Compared structures

  • 6IKZ · UDP-glucose pyrophosphorylase from acinetobacter baumanii · the same entry in another collection · chain B against B, TM-score 1.00

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