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Structural and functional characterisation of a bacterial laccase-like multi-copper oxidase cueo from lignin-degrading bacterium ochrobactrum sp. with oxidase activity towards lignin model compounds and lignosulfonate

Analyse Structural and functional characterisation of a bacterial laccase-like… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6EVG
Type
protein
Length
444 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Multi-copper oxidase cueo
EC
1.10.3.2
Ligands
CU
Pockets
1 · best druggability 0.43

Structure

x-ray diffraction · 1 distinct chain · 9% helix, 41% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AMulti-copper oxidase cueo (EC 1.10.3.2)protein4449% helix, 41% strand—

Ligands and binding sites

  • CU · Copper (II) ion · metal · chains A
  • EDO · 1,2-ethanediol · additive · 2 copies · chains A

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

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11320.430.7622EDO

Compared structures

  • 6EVG · Structural and Functional Characterisation of a Bacterial Laccase-like Multi-copper… · the same entry in another collection · chain A against A, TM-score 1.00

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