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Crystal structure of laccase from cerrena maxima at 1.9A resolution

Analyse Crystal structure of laccase from cerrena maxima at 1.9A resolution in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2H5U
Type
protein
Length
499 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Laccase
EC
1.10.3.2
Ligands
NAG, MAN, CU
Pockets
5 · best druggability 0.54

Structure

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

ChainMoleculeTypeResiduesSecondary structureUniProt
ALaccase (EC 1.10.3.2)protein49911% helix, 38% strand—

Ligands and binding sites

  • NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 6 copies · chains A
  • MAN · alpha-D-mannopyranose · sugar · 4 copies · chains A
  • CU · Copper (II) ion · metal · 4 copies · 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, 1 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11210.540.8222empty
21170.420.7616empty
3850.420.7918empty
41110.370.7417empty
5570.300.7516empty

Modifications

Observed in the structure: 4 glycan, 2 disulfide, 2 modified (N-glycosylation, disulfide, nonstandard).

Compared structures

  • 2H5U · Crystal structure of laccase from Cerrena maxima at 1.9A resolution · the same entry in another collection · chain A against A, TM-score 1.00

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