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Crystal structure of orotidine monophosphate decarboxylase complexed with cmp

Analyse Crystal structure of orotidine monophosphate decarboxylase complexed with cmp in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1LP6
Type
protein
Length
418 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Orotidine monophosphate decarboxylase
EC
4.1.1.23
UniProt
O26232
Ligands
C5P
Pockets
4 · best druggability 0.66

Structure

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

ChainMoleculeTypeResiduesSecondary structureUniProt
AOrotidine monophosphate decarboxylase (EC 4.1.1.23)protein20448% helix, 19% strandO26232
BOrotidine monophosphate decarboxylase (EC 4.1.1.23)protein21452% helix, 18% strandO26232

Ligands and binding sites

  • C5P · Cytidine-5'-monophosphate · ligand · 2 copies · chains A, B

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13410.660.8138C5P
22320.640.8233C5P
3830.410.7814empty
4610.350.7712empty

Interfaces

1 interface between chains.

  • A–B · 1651 Ų buried · 14 hydrogen bonds · protein-protein

Compared structures

  • 1LP6 · Crystal structure of orotidine monophosphate decarboxylase complexed with CMP · the same entry in another collection · chain A against A, TM-score 1.00

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