GL1X · GenesisL1 explorer

Research workbench

Crystal structure of laccases from pycnoporus sanguineus, izoform II

Analyse Crystal structure of laccases from pycnoporus sanguineus, izoform II in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5NQ8
Type
protein
Length
497 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Laccase
UniProt
Q96TR6
Ligands
ME2, IPH, NAG, MAN, BMA, CU, NA, PER
Pockets
4 · best druggability 0.50

Structure

x-ray diffraction · 1 distinct chain · 11% helix, 38% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ALaccaseprotein49711% helix, 38% strandQ96TR6

Ligands and binding sites

  • ME2 · 1-ethoxy-2-(2-methoxyethoxy)ethane · ligand · 2 copies · chains A
  • IPH · Phenol · ligand · chains A
  • NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 4 copies · chains A
  • MAN · alpha-D-mannopyranose · sugar
  • BMA · beta-D-mannopyranose · sugar
  • CU · Copper (II) ion · metal · 4 copies · chains A
  • NA · Sodium ion · metal · 2 copies · chains A
  • PER · Peroxide ion · ion · chains A
  • MLI · Malonate ion · additive · 3 copies · 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, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11150.500.8017empty
21960.470.7531NA
3900.430.7919empty
41200.370.7419empty

Modifications

Observed in the structure: 2 disulfide, 2 glycan (disulfide, N-glycosylation).

Compared structures

  • 5NQ8 · Crystal structure of laccases from Pycnoporus sanguineus, izoform II · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.