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Crystal structure of lysine decarboxylase from selenomonas ruminantium in P43212 space group

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

PDB
5GJN
Type
protein
Length
369 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
LYSINE/ORNITHINE decarboxylase
EC
4.1.1.18
UniProt
O50657
Ligands
MG
Pockets
2 · best druggability 0.49

Structure

x-ray diffraction · 1 distinct chain · 38% helix, 22% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ALYSINE/ORNITHINE decarboxylase (EC 4.1.1.18)protein36938% helix, 22% strandO50657

Ligands and binding sites

  • MG · Magnesium ion · metal · 2 copies · chains A
  • GOL · Glycerol · additive · 2 copies · chains A
  • 1PE · Pentaethylene glycol · additive · chains A
  • PGE · Triethylene glycol · 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, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12140.490.7532GOL, MG
2660.310.7413empty

Compared structures

  • 5GJN · Crystal structure of Lysine decarboxylase from Selenomonas ruminantium in P43212 space… · 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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