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Crystal structure of the francisella novicida lysine decarboxylase ldcf

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

PDB
6Y3X
Type
protein
Length
3,585 residues
Chains
5
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Lysine decarboxylase
UniProt
A0Q584
Pockets
20 · best druggability 0.75

Structure

x-ray diffraction · 1 distinct chain · 41% helix, 16% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, D, ELysine decarboxylaseprotein71741% helix, 16% strandA0Q584

Pockets

20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
110080.750.78103empty
29750.750.7893empty
36350.750.8179empty
46490.740.8167empty
52240.660.8441empty

Interfaces

5 interfaces between chains.

  • A–C · 1214 Ų buried · 11 hydrogen bonds · protein-protein
  • B–E · 1157 Ų buried · 11 hydrogen bonds · protein-protein
  • C–E · 1142 Ų buried · 9 hydrogen bonds · protein-protein
  • B–D · 1139 Ų buried · 12 hydrogen bonds · protein-protein
  • A–D · 1102 Ų buried · 10 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 5 modified (cofactor).

Compared structures

  • 6Y3X · Crystal structure of the Francisella novicida lysine decarboxylase LdcF · the same entry in another collection · chain A against A, TM-score 1.00

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