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Crystal structure of a feruloyl esterase LP_0796 from Lactobacillus plantarum

Analyse Crystal structure of a feruloyl esterase LP_0796 from Lactobacillus plantarum in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7EBO
Type
protein
Length
484 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v2 / PDB Bank
Contract
0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner
0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution
2.5
Source
Lactiplantibacillus plantarum WCFS1
Molecule
Carboxylesterase
EC
3.1.1.1
UniProt
F9UM18
Ligands
SO4
Pockets
4 · best druggability 0.78

Structure

x-ray diffraction · resolution 2.5 · 2 distinct chains · 50% helix, 15% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ACarboxylesterase (EC 3.1.1.1)protein24252% helix, 15% strandF9UM18
BCarboxylesterase (EC 3.1.1.1)protein24248% helix, 14% strandF9UM18

Ligands and binding sites

  • SO4 · Sulfate ion · ion · chains A

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
15050.780.8545empty
21110.680.9116empty
32090.620.8228empty
41150.580.8534empty

Interfaces

1 interface between chains.

  • A–B · 1648 Ų buried · 17 hydrogen bonds · protein-protein

Compared structures

  • 7EBO · Crystal structure of a feruloyl esterase LP_0796 from lactobacillus plantarum · the same entry in another collection · chain A against A, TM-score 1.00

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