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Crystal structure of the oxy-form of the copper-bound streptomyces castaneoglobisporus tyrosinase complexed with a caddie protein prepared by the addition of dithiothreitol

Analyse Crystal structure of the oxy-form of the copper-bound streptomyces… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1WX4
Type
protein
Length
344 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Tyrosinase; Melc
EC
1.14.18.1
UniProt
Q83WS2, Q83WS1
Ligands
CU, NO3, PER
Pockets
1 · best druggability 0.47

Structure

x-ray diffraction · 2 distinct chains · 37% helix, 13% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ATyrosinase (EC 1.14.18.1)protein27342% helix, 4% strandQ83WS2
BMelcprotein7117% helix, 46% strandQ83WS1

Ligands and binding sites

  • CU · Copper (II) ion · metal · 4 copies · chains A, B
  • NO3 · Nitrate ion · ion · 5 copies · chains A, B
  • PER · Peroxide ion · ion · chains A, B

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

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11130.470.7925empty

Interfaces

1 interface between chains.

  • A–B · 1021 Ų buried · 16 hydrogen bonds · protein-protein

Compared structures

  • 1WX4 · Crystal structure of the oxy-form of the copper-bound Streptomyces castaneoglobisporus… · the same entry in another collection · chain A against A, TM-score 1.00

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