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Crystal structure of udp-N-acetylglucosamine 1-carboxyvinyltransferase from aquifex aeolicus VF5

Analyse Crystal structure of udp-N-acetylglucosamine 1-carboxyvinyltransferase from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2YVW
Type
protein
Length
416 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Udp-N-acetylglucosamine 1-carboxyvinyltransferase
EC
2.5.1.7
UniProt
O67315
Ligands
EPU, PO4
Pockets
2 · best druggability 0.79

Structure

x-ray diffraction · 1 distinct chain · 34% helix, 28% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AUdp-N-acetylglucosamine 1-carboxyvinyltransferase (EC 2.5.1.7)protein41634% helix, 28% strandO67315

Ligands and binding sites

  • EPU · Uridine-diphosphate-2(N-acetylglucosaminyl) butyric acid · ligand · chains A
  • PO4 · Phosphate ion · ion · chains A

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
15410.790.8562PO4, EPU
2590.260.7219empty

Compared structures

  • 2YVW · Crystal structure of UDP-N-acetylglucosamine 1-carboxyvinyltransferase from Aquifex… · the same entry in another collection · chain A against A, TM-score 1.00
  • O67315 · AlphaFold monomer V2.0 prediction for udp-N-acetylglucosamine 1-carboxyvinyltransferase… · a predicted model of the same protein · chain A against A, TM-score 1.00

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