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Inducible lysine decarboxylase ldci decamer, pH 7.0

Analyse Inducible lysine decarboxylase ldci decamer, pH 7.0 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6YN5
Type
protein
Length
7,110 residues
Chains
10
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Inducible lysine decarboxylase
EC
4.1.1.18
UniProt
P0A9H3
Pockets
20 · best druggability 0.85

Structure

electron microscopy · 1 distinct chain · 42% helix, 17% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, D, E, F, G, H, I, JInducible lysine decarboxylase (EC 4.1.1.18)protein71142% helix, 17% strandP0A9H3

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
111690.850.86116empty
211080.850.86110empty
310210.850.86114empty
411270.850.86118empty
59160.830.8578empty

Interfaces

20 interfaces between chains.

  • E–I · 5185 Ų buried · 58 hydrogen bonds · protein-protein
  • D–J · 5182 Ų buried · 56 hydrogen bonds · protein-protein
  • B–G · 5164 Ų buried · 51 hydrogen bonds · protein-protein
  • C–F · 5161 Ų buried · 53 hydrogen bonds · protein-protein
  • A–H · 5142 Ų buried · 50 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 10 modified (cofactor).

Compared structures

  • 6YN5 · Inducible lysine decarboxylase LdcI decamer, pH 7.0 · the same entry in another collection · chain J against J, TM-score 1.00
  • P0A9H3 · AlphaFold monomer V2.0 prediction for inducible lysine decarboxylase (P0A9H3) · a predicted model of the same protein · chain A against A, TM-score 1.00

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