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Crystal structure of saccharomyces cerevisiae omp synthase in complex with PRP(CH2)P

Analyse Crystal structure of saccharomyces cerevisiae omp synthase in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4WML
Type
protein
Length
216 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Orotate phosphoribosyltransferase 1
EC
2.4.2.10
UniProt
P13298
Ligands
PPC, MG
Pockets
2 · best druggability 0.53

Structure

x-ray diffraction · 1 distinct chain · 44% helix, 23% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AOrotate phosphoribosyltransferase 1 (EC 2.4.2.10)protein21644% helix, 23% strandP13298

Ligands and binding sites

  • PPC · 1-O-[(R)-hydroxy(phosphonomethyl)phosphoryl]-5-O-phosphono-alpha-D-ribofuranose · ligand · chains A
  • MG · Magnesium ion · metal · 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
12130.530.7725empty
2870.380.7615empty

Compared structures

  • 4WML · Crystal structure of Saccharomyces cerevisiae OMP synthase in complex with PRP(CH2)P · the same entry in another collection · chain A against A, TM-score 1.00
  • P13298 · AlphaFold monomer V2.0 prediction for orotate phosphoribosyltransferase 1 (P13298) · a predicted model of the same protein · chain A against A, TM-score 0.96

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