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Copper in PDB 1wx4: Crystal Structure of the Oxy-Form of the Copper-Bound Streptomyces Castaneoglobisporus Tyrosinase Complexed with A Caddie Protein Prepared By the Addition of Dithiothreitol

Enzymatic activity of Crystal Structure of the Oxy-Form of the Copper-Bound Streptomyces Castaneoglobisporus Tyrosinase Complexed with A Caddie Protein Prepared By the Addition of Dithiothreitol

All present enzymatic activity of Crystal Structure of the Oxy-Form of the Copper-Bound Streptomyces Castaneoglobisporus Tyrosinase Complexed with A Caddie Protein Prepared By the Addition of Dithiothreitol:
1.14.18.1;

Protein crystallography data

The structure of Crystal Structure of the Oxy-Form of the Copper-Bound Streptomyces Castaneoglobisporus Tyrosinase Complexed with A Caddie Protein Prepared By the Addition of Dithiothreitol, PDB code: 1wx4 was solved by Y.Matoba, T.Kumagai, A.Yamamoto, H.Yoshitsu, M.Sugiyama, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.00 / 1.50
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 65.360, 98.230, 55.170, 90.00, 90.00, 90.00
R / Rfree (%) 18.8 / 21.6

Copper Binding Sites:

The binding sites of Copper atom in the Crystal Structure of the Oxy-Form of the Copper-Bound Streptomyces Castaneoglobisporus Tyrosinase Complexed with A Caddie Protein Prepared By the Addition of Dithiothreitol (pdb code 1wx4). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 4 binding sites of Copper where determined in the Crystal Structure of the Oxy-Form of the Copper-Bound Streptomyces Castaneoglobisporus Tyrosinase Complexed with A Caddie Protein Prepared By the Addition of Dithiothreitol, PDB code: 1wx4:
Jump to Copper binding site number: 1; 2; 3; 4;

Copper binding site 1 out of 4 in 1wx4

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Copper binding site 1 out of 4 in the Crystal Structure of the Oxy-Form of the Copper-Bound Streptomyces Castaneoglobisporus Tyrosinase Complexed with A Caddie Protein Prepared By the Addition of Dithiothreitol


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Crystal Structure of the Oxy-Form of the Copper-Bound Streptomyces Castaneoglobisporus Tyrosinase Complexed with A Caddie Protein Prepared By the Addition of Dithiothreitol within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu400

b:24.7
occ:1.00
O2 A:PER409 2.0 20.3 1.0
O1 A:PER409 2.0 22.2 1.0
NE2 A:HIS38 2.1 15.7 1.0
NE2 A:HIS54 2.2 19.7 1.0
NE2 A:HIS63 2.4 10.3 1.0
CD2 A:HIS54 2.8 16.7 1.0
CE1 A:HIS63 3.0 9.5 1.0
CE1 A:HIS38 3.1 14.7 1.0
CD2 A:HIS38 3.1 13.8 1.0
CE1 A:HIS54 3.3 18.1 1.0
CU A:CU401 3.6 15.3 1.0
CD2 A:HIS63 3.6 8.9 1.0
OH B:TYR98 4.0 16.5 1.0
CG A:HIS54 4.1 16.6 1.0
NE2 A:HIS216 4.1 10.3 1.0
ND1 A:HIS38 4.2 13.8 1.0
CG A:HIS38 4.2 13.7 1.0
ND1 A:HIS63 4.2 9.6 1.0
ND1 A:HIS54 4.3 17.5 1.0
CE2 A:PHE212 4.4 8.8 1.0
CE1 A:HIS216 4.5 8.1 1.0
CZ A:PHE212 4.5 7.7 1.0
CD1 A:ILE42 4.5 18.4 1.0
CG A:HIS63 4.6 9.4 1.0
CE2 B:TYR98 4.8 14.4 1.0
CZ B:TYR98 4.9 14.7 1.0
NE2 A:HIS190 4.9 8.0 1.0
CE1 A:PHE59 4.9 7.5 1.0

Copper binding site 2 out of 4 in 1wx4

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Copper binding site 2 out of 4 in the Crystal Structure of the Oxy-Form of the Copper-Bound Streptomyces Castaneoglobisporus Tyrosinase Complexed with A Caddie Protein Prepared By the Addition of Dithiothreitol


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of Crystal Structure of the Oxy-Form of the Copper-Bound Streptomyces Castaneoglobisporus Tyrosinase Complexed with A Caddie Protein Prepared By the Addition of Dithiothreitol within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu401

b:15.3
occ:1.00
O2 A:PER409 2.0 20.3 1.0
O1 A:PER409 2.0 22.2 1.0
NE2 A:HIS190 2.1 8.0 1.0
NE2 A:HIS194 2.1 11.3 1.0
NE2 A:HIS216 2.2 10.3 1.0
CE1 A:HIS190 3.0 8.6 1.0
CE1 A:HIS216 3.0 8.1 1.0
CE1 A:HIS194 3.0 10.3 1.0
CD2 A:HIS194 3.1 10.4 1.0
CD2 A:HIS190 3.1 7.8 1.0
CD2 A:HIS216 3.3 8.7 1.0
CU A:CU400 3.6 24.7 1.0
CE2 B:TYR98 3.9 14.4 1.0
OH B:TYR98 4.0 16.5 1.0
ND1 A:HIS190 4.1 8.4 1.0
ND1 A:HIS194 4.1 11.0 1.0
CG A:HIS194 4.2 9.3 1.0
ND1 A:HIS216 4.2 7.6 1.0
CG A:HIS190 4.2 9.0 1.0
CZ B:TYR98 4.2 14.7 1.0
CG A:HIS216 4.3 8.3 1.0
CE2 A:PHE212 4.3 8.8 1.0
NE2 A:HIS63 4.4 10.3 1.0
CD2 A:HIS215 4.6 9.5 1.0
CE1 A:PHE59 4.8 7.5 1.0
NE2 A:HIS215 4.8 9.1 1.0
CD2 B:TYR98 4.8 14.3 1.0
NE2 A:HIS38 4.8 15.7 1.0
CD2 A:HIS63 4.9 8.9 1.0
CD2 A:PHE212 5.0 7.8 1.0
CZ A:PHE212 5.0 7.7 1.0

Copper binding site 3 out of 4 in 1wx4

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Copper binding site 3 out of 4 in the Crystal Structure of the Oxy-Form of the Copper-Bound Streptomyces Castaneoglobisporus Tyrosinase Complexed with A Caddie Protein Prepared By the Addition of Dithiothreitol


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 3 of Crystal Structure of the Oxy-Form of the Copper-Bound Streptomyces Castaneoglobisporus Tyrosinase Complexed with A Caddie Protein Prepared By the Addition of Dithiothreitol within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu403

b:56.9
occ:0.50
O A:HOH707 2.8 31.5 0.5
O A:HOH725 4.9 33.5 1.0
CG A:PRO231 4.9 20.5 1.0

Copper binding site 4 out of 4 in 1wx4

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Copper binding site 4 out of 4 in the Crystal Structure of the Oxy-Form of the Copper-Bound Streptomyces Castaneoglobisporus Tyrosinase Complexed with A Caddie Protein Prepared By the Addition of Dithiothreitol


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 4 of Crystal Structure of the Oxy-Form of the Copper-Bound Streptomyces Castaneoglobisporus Tyrosinase Complexed with A Caddie Protein Prepared By the Addition of Dithiothreitol within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu402

b:48.0
occ:1.00
NE2 B:HIS82 2.1 32.6 1.0
CD2 B:HIS82 2.9 26.7 1.0
CE1 B:HIS82 3.2 26.8 1.0
O A:HOH751 3.4 28.6 1.0
CG B:HIS82 4.1 23.7 1.0
ND1 B:HIS82 4.2 25.8 1.0
O A:MET43 4.3 16.6 1.0
O B:HOH596 5.0 20.9 1.0

Reference:

Y.Matoba, T.Kumagai, A.Yamamoto, H.Yoshitsu, M.Sugiyama. Crystallographic Evidence That the Dinuclear Copper Center of Tyrosinase Is Flexible During Catalysis J.Biol.Chem. V. 281 8981 2006.
ISSN: ISSN 0021-9258
PubMed: 16436386
DOI: 10.1074/JBC.M509785200
Page generated: Sun Dec 13 11:02:50 2020

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