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Crystal structure of laccase from lentinus sp. at 1.8 a resolution

Analyse Crystal structure of laccase from lentinus sp. at 1.8 a resolution in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3X1B
Type
protein
Length
1,000 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Laccase
EC
1.10.3.2
Ligands
MAN, NAG, BMA, CU
Pockets
10 · best druggability 0.83

Structure

x-ray diffraction · 1 distinct chain · 11% helix, 39% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BLaccase (EC 1.10.3.2)protein50011% helix, 39% strand—

Ligands and binding sites

  • MAN · alpha-D-mannopyranose · sugar · 13 copies · chains A, B
  • NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 10 copies · chains A, B
  • BMA · beta-D-mannopyranose · sugar · 4 copies
  • CU · Copper (II) ion · metal · 8 copies · chains A, B

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

Pockets

10 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
110210.830.83111empty
24810.700.8070empty
32570.540.7642empty
42590.540.7642empty
51290.520.8119empty

Interfaces

1 interface between chains.

  • A–B · 1004 Ų buried · 9 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 6 glycan, 4 disulfide (N-glycosylation, disulfide).

Compared structures

  • 3X1B · Crystal structure of laccase from Lentinus sp. at 1.8 A resolution · the same entry in another collection · chain A against A, TM-score 1.00

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