GL1X · GenesisL1 explorer

Research workbench

Two-domain laccase from streptomyces viridochromogenes at 2.4 a resolution AC629

Analyse Two-domain laccase from streptomyces viridochromogenes at 2.4 a resolution AC629 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4N8U
Type
protein
Length
826 residues
Chains
3
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Multicopper oxidase
EC
1.10.3.2
UniProt
J9S5G3
Ligands
CU, CL
Pockets
8 · best druggability 0.84

Structure

x-ray diffraction · 2 distinct chains · 5% helix, 42% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, CMulticopper oxidase (EC 1.10.3.2)protein2755% helix, 42% strandJ9S5G3
BMulticopper oxidase (EC 1.10.3.2)protein2765% helix, 42% strandJ9S5G3

Ligands and binding sites

  • CU · Copper (II) ion · metal · 9 copies · chains A, B, C
  • CL · Chloride ion · ion · 6 copies · chains A, B, C
  • TRS · 2-amino-2-hydroxymethyl-propane-1,3-diol · additive · chains B

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

Pockets

8 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13660.840.9344empty
2670.720.9820empty
32750.690.8453empty
42730.660.8351empty
52160.580.8037empty

Interfaces

3 interfaces between chains.

  • B–C · 1889 Ų buried · 33 hydrogen bonds · protein-protein
  • A–B · 1823 Ų buried · 30 hydrogen bonds · protein-protein
  • A–C · 1806 Ų buried · 34 hydrogen bonds · protein-protein

Compared structures

  • 4N8U · Two-Domain Laccase from Streptomyces viridochromogenes at 2.4 A resolution AC629 · 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.