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Human ompd-domain of umps in complex with the substrate omp at 1.25 ångströms resolution, 3.55 mgy exposure

Analyse Human ompd-domain of umps in complex with the substrate omp at 1.25 ångströms… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6YVO
Type
protein
Length
256 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Uridine 5'-monophosphate synthase
EC
2.4.2.10, 4.1.1.23
UniProt
P11172
Ligands
OMP, U, SO4
Pockets
1 · best druggability 0.52

Structure

x-ray diffraction · 1 distinct chain · 45% helix, 18% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AUridine 5'-monophosphate synthase (EC 2.4.2.10, 4.1.1.23)protein25645% helix, 18% strandP11172

Ligands and binding sites

  • OMP · Orotidine-5'-monophosphate · ligand · chains A
  • U · Uridine-5'-monophosphate · ligand · chains A
  • SO4 · Sulfate ion · ion · 6 copies · 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
11570.520.7928OMP, U

Modifications

Observed in the structure: 2 modified (acetylation, oxidation).

Compared structures

  • 6YVO · Human OMPD-domain of UMPS in complex with the substrate OMP at 1.25 Angstroms resolution… · the same entry in another collection · chain A against A, TM-score 1.00

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