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Crystal structure of lysine decarboxylase from selenomonas ruminantium in C2 space group

Analyse Crystal structure of lysine decarboxylase from selenomonas ruminantium in C2… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5GJM
Type
protein
Length
749 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
LYSINE/ORNITHINE decarboxylase
EC
4.1.1.18
UniProt
O50657
Pockets
10 · best druggability 0.73

Structure

x-ray diffraction · 2 distinct chains · 36% helix, 22% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ALYSINE/ORNITHINE decarboxylase (EC 4.1.1.18)protein38135% helix, 22% strandO50657
BLYSINE/ORNITHINE decarboxylase (EC 4.1.1.18)protein36837% helix, 22% strandO50657

Ligands and binding sites

  • GOL · Glycerol · additive · chains A

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

Pockets

10 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
14830.730.8353empty
24560.670.7945empty
3780.660.9227empty
4570.640.9429empty
53790.600.7650empty

Interfaces

1 interface between chains.

  • A–B · 2539 Ų buried · 34 hydrogen bonds · protein-protein

Compared structures

  • 5GJM · Crystal structure of Lysine decarboxylase from Selenomonas ruminantium in C2 space group · the same entry in another collection · chain A against A, TM-score 1.00
  • O50657 · AlphaFold monomer V2.0 prediction for LYSINE/ORNITHINE decarboxylase (O50657) · a predicted model of the same protein · chain A against A, TM-score 0.98

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