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OMPD-domain of human UMPS in complex with 6-thiocarboxamido-UMP at 1.15 Angstroms resolution

Analyse OMPD-domain of human UMPS in complex with 6-thiocarboxamido-UMP at 1.15… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6ZX3
Type
protein
Length
256 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v2 / PDB Bank
Contract
0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner
0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution
1.15
Source
Homo sapiens
Molecule
Uridine 5'-monophosphate synthase
EC
2.4.2.10, 4.1.1.23
UniProt
P11172
Ligands
QRZ, PRO, SO4
Pockets
1 · best druggability 0.57

Structure

x-ray diffraction · resolution 1.15 · 1 distinct chain · 44% helix, 18% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AUridine 5'-monophosphate synthase (EC 2.4.2.10, 4.1.1.23)protein25644% helix, 18% strandP11172

Ligands and binding sites

  • QRZ · [(2~{R},3~{S},4~{R},5~{R})-5-[6-carbamothioyl-2,4-bis(oxidanylidene)pyrimidin-1-yl]-3,4-bis(oxidanyl) oxolan-2-yl]methyl dihydrogen phosphate · ligand · chains A
  • PRO · Proline · ligand · chains A
  • SO4 · Sulfate ion · ion · chains A
  • GOL · Glycerol · additive · chains A

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12480.570.7938QRZ

Compared structures

  • 6ZX3 · Ompd-domain of human umps in complex with 6-thiocarboxamido-ump at 1.15 ångströms… · the same entry in another collection · chain A against A, TM-score 1.00
  • P11172 · AlphaFold monomer V2.0 prediction for uridine 5'-monophosphate synthase (P11172) · a predicted model of the same protein · chain A against A, TM-score 1.00

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