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Type-2 cu-depleted laccase from coprinus cinereus

Analyse Type-2 cu-depleted laccase from coprinus cinereus in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1A65
Type
protein
Length
504 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Laccase
EC
1.10.3.2
UniProt
Q9Y780
Ligands
PYE, NAG, CU, O
Pockets
5 · best druggability 0.53

Structure

x-ray diffraction · 1 distinct chain · 13% helix, 38% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ALaccase (EC 1.10.3.2)protein50413% helix, 38% strandQ9Y780

Ligands and binding sites

  • PYE · Tetrahydropyran · ligand · chains A
  • NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · chains A
  • CU · Copper (II) ion · metal · 3 copies · chains A
  • O · Oxygen atom · ion · chains A

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

Pockets

5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11930.530.7826empty
22250.520.7734empty
31010.470.8018empty
41120.440.7815empty
5690.310.7423empty

Modifications

Observed in the structure: 2 disulfide, 1 covalent, 1 glycan (disulfide, covalent ligand, N-glycosylation).

Compared structures

  • 1A65 · Type-2 cu-depleted laccase from coprinus cinereus · the same entry in another collection · chain A against A, TM-score 1.00

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