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Radiation damage in Aspergillus oryzae pro-tyrosinase oxygen-bound C92A/H103F mutant

Analyse Radiation damage in Aspergillus oryzae pro-tyrosinase oxygen-bound C92A/H103F… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6JUD
Type
protein
Length
1,084 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v2 / PDB Bank
Contract
0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner
0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution
1.56
Source
Aspergillus oryzae
Molecule
Tyrosinase
EC
1.14.18.1
UniProt
A0A1S9DK56
Ligands
CU, PER
Pockets
14 · best druggability 0.77

Structure

x-ray diffraction · resolution 1.56 · 2 distinct chains · 36% helix, 17% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ATyrosinase (EC 1.14.18.1)protein53336% helix, 17% strandA0A1S9DK56
BTyrosinase (EC 1.14.18.1)protein55136% helix, 17% strandA0A1S9DK56

Ligands and binding sites

  • CU · Copper (II) ion · metal · 4 copies · chains A, B
  • PER · Peroxide ion · ion · chains B

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11050.770.9728empty
2990.750.9622empty
38090.700.7686empty
4520.690.9819empty
5540.680.9719empty

Interfaces

1 interface between chains.

  • A–B · 1535 Ų buried · 12 hydrogen bonds · protein-protein

Compared structures

  • 6JUD · Radiation damage in aspergillus oryzae pro-tyrosinase oxygen-bound C92A/H103F mutant · the same entry in another collection · chain A against A, TM-score 1.00

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