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Crystal structure of orotidine 5'-monophosphate decarboxylase from methanobacterium thermoautotrophicum complexed with 6-azauridine 5'- monophosphate

Analyse Crystal structure of orotidine 5'-monophosphate decarboxylase from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4NX5
Type
protein
Length
439 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Orotidine 5'-phosphate decarboxylase
EC
4.1.1.23
UniProt
O26232
Ligands
UP6, MG, CL
Pockets
2 · best druggability 0.78

Structure

x-ray diffraction · 2 distinct chains · 50% helix, 19% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AOrotidine 5'-phosphate decarboxylase (EC 4.1.1.23)protein22049% helix, 19% strandO26232
BOrotidine 5'-phosphate decarboxylase (EC 4.1.1.23)protein21952% helix, 19% strandO26232

Ligands and binding sites

  • UP6 · 6-aza uridine 5'-monophosphate · ligand · 2 copies · chains A, B
  • MG · Magnesium ion · metal · 2 copies · chains B
  • CL · Chloride ion · ion · 4 copies · chains A, B
  • GOL · Glycerol · additive · 2 copies · chains B
  • EDO · 1,2-ethanediol · additive · 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, 2 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11160.780.9733UP6
21230.780.9633UP6

Interfaces

1 interface between chains.

  • A–B · 1758 Ų buried · 19 hydrogen bonds · protein-protein

Compared structures

  • 4NX5 · Crystal structure of orotidine 5'-monophosphate decarboxylase from methanobacterium… · the same entry in another collection · chain A against A, TM-score 1.00

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