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Crystal structure of orotidine monophosphate decarboxylase complexed with 6-azaump

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

PDB
1DVJ
Type
protein
Length
900 residues
Chains
4
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
Pockets
9 · best druggability 0.57

Structure

x-ray diffraction · 4 distinct chains · 52% helix, 18% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AOrotidine 5'-phosphate decarboxylase (EC 4.1.1.23)protein23953% helix, 17% strandO26232
BOrotidine 5'-phosphate decarboxylase (EC 4.1.1.23)protein21152% helix, 19% strandO26232
COrotidine 5'-phosphate decarboxylase (EC 4.1.1.23)protein23652% helix, 17% strandO26232
DOrotidine 5'-phosphate decarboxylase (EC 4.1.1.23)protein21450% helix, 19% strandO26232

Ligands and binding sites

  • UP6 · 6-aza uridine 5'-monophosphate · ligand · 4 copies · chains A, B, C, D

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11870.570.8027UP6
21840.560.8029UP6
31930.560.8028UP6
41670.550.8029UP6
51370.450.7723empty

Interfaces

1 interface between chains.

  • A–B · 297 Ų buried · 2 hydrogen bonds · protein-protein

Compared structures

  • 1DVJ · Crystal structure of orotidine monophosphate decarboxylase complexed with 6-azaump · the same entry in another collection · chain A against A, TM-score 1.00

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