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Copper in PDB 2zmx: Crystal Structure of the MET1-Form of the Copper-Bound Tyrosinase in Complex with A Caddie Protein From Streptomyces Castaneoglobisporus Obtained By Soaking in Cupric Sulfate Solution For 36 Hours

Enzymatic activity of Crystal Structure of the MET1-Form of the Copper-Bound Tyrosinase in Complex with A Caddie Protein From Streptomyces Castaneoglobisporus Obtained By Soaking in Cupric Sulfate Solution For 36 Hours

All present enzymatic activity of Crystal Structure of the MET1-Form of the Copper-Bound Tyrosinase in Complex with A Caddie Protein From Streptomyces Castaneoglobisporus Obtained By Soaking in Cupric Sulfate Solution For 36 Hours:
1.14.18.1;

Protein crystallography data

The structure of Crystal Structure of the MET1-Form of the Copper-Bound Tyrosinase in Complex with A Caddie Protein From Streptomyces Castaneoglobisporus Obtained By Soaking in Cupric Sulfate Solution For 36 Hours, PDB code: 2zmx was solved by Y.Matoba, M.Sugiyama, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.00 / 1.33
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 65.240, 98.020, 55.170, 90.00, 90.00, 90.00
R / Rfree (%) 17.6 / 21.3

Copper Binding Sites:

The binding sites of Copper atom in the Crystal Structure of the MET1-Form of the Copper-Bound Tyrosinase in Complex with A Caddie Protein From Streptomyces Castaneoglobisporus Obtained By Soaking in Cupric Sulfate Solution For 36 Hours (pdb code 2zmx). 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 MET1-Form of the Copper-Bound Tyrosinase in Complex with A Caddie Protein From Streptomyces Castaneoglobisporus Obtained By Soaking in Cupric Sulfate Solution For 36 Hours, PDB code: 2zmx:
Jump to Copper binding site number: 1; 2; 3; 4;

Copper binding site 1 out of 4 in 2zmx

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Copper binding site 1 out of 4 in the Crystal Structure of the MET1-Form of the Copper-Bound Tyrosinase in Complex with A Caddie Protein From Streptomyces Castaneoglobisporus Obtained By Soaking in Cupric Sulfate Solution For 36 Hours


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 MET1-Form of the Copper-Bound Tyrosinase in Complex with A Caddie Protein From Streptomyces Castaneoglobisporus Obtained By Soaking in Cupric Sulfate Solution For 36 Hours within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu301

b:31.6
occ:1.00
NE2 A:HIS38 2.0 17.5 1.0
NE2 A:HIS54 2.0 19.8 1.0
O B:HOH310 2.2 9.7 0.3
O B:HOH310 2.2 10.8 0.7
NE2 A:HIS63 2.4 10.4 1.0
CE1 A:HIS38 2.8 18.8 1.0
CD2 A:HIS54 2.9 19.8 1.0
CE1 A:HIS63 3.0 10.2 1.0
CE1 A:HIS54 3.0 18.5 1.0
CD2 A:HIS38 3.0 17.7 1.0
CD2 A:HIS63 3.6 10.3 1.0
CU A:CU302 3.7 18.7 1.0
ND1 A:HIS38 4.0 14.2 1.0
CG A:HIS54 4.1 19.6 1.0
OH B:TYR98 4.1 19.6 1.0
CD1 A:ILE42 4.1 36.8 1.0
CG A:HIS38 4.1 14.1 1.0
ND1 A:HIS54 4.1 17.1 1.0
NE2 A:HIS216 4.1 11.6 1.0
ND1 A:HIS63 4.3 9.3 1.0
CZ A:PHE212 4.3 9.5 1.0
CE2 A:PHE212 4.4 10.0 1.0
CE1 A:HIS216 4.5 10.9 1.0
CG A:HIS63 4.6 8.5 1.0
CE1 A:PHE59 5.0 11.0 1.0

Copper binding site 2 out of 4 in 2zmx

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Copper binding site 2 out of 4 in the Crystal Structure of the MET1-Form of the Copper-Bound Tyrosinase in Complex with A Caddie Protein From Streptomyces Castaneoglobisporus Obtained By Soaking in Cupric Sulfate Solution For 36 Hours


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 MET1-Form of the Copper-Bound Tyrosinase in Complex with A Caddie Protein From Streptomyces Castaneoglobisporus Obtained By Soaking in Cupric Sulfate Solution For 36 Hours within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu302

b:18.7
occ:1.00
O B:HOH310 1.9 10.8 0.7
NE2 A:HIS190 2.0 12.0 1.0
NE2 A:HIS194 2.0 8.7 1.0
NE2 A:HIS216 2.1 11.6 1.0
O B:HOH310 2.2 9.7 0.3
CE1 A:HIS190 3.0 11.7 1.0
CE1 A:HIS216 3.0 10.9 1.0
CE1 A:HIS194 3.0 10.0 1.0
CD2 A:HIS190 3.0 11.1 1.0
CD2 A:HIS194 3.1 9.4 1.0
CD2 A:HIS216 3.2 12.2 1.0
CU A:CU301 3.7 31.6 1.0
CE2 B:TYR98 3.9 15.8 1.0
OH B:TYR98 4.0 19.6 1.0
ND1 A:HIS190 4.1 9.7 1.0
CG A:HIS190 4.1 9.3 1.0
ND1 A:HIS194 4.1 9.8 1.0
ND1 A:HIS216 4.1 10.9 1.0
CG A:HIS194 4.2 9.2 1.0
CZ B:TYR98 4.2 15.5 1.0
CE2 A:PHE212 4.2 10.0 1.0
CG A:HIS216 4.3 10.1 1.0
CD2 A:HIS215 4.5 12.6 1.0
NE2 A:HIS63 4.6 10.4 1.0
NE2 A:HIS215 4.7 11.8 1.0
CE1 A:PHE59 4.8 11.0 1.0
CD2 B:TYR98 4.8 14.6 1.0
CZ A:PHE212 4.8 9.5 1.0
NE2 A:HIS38 4.9 17.5 1.0
CD2 A:PHE212 4.9 9.8 1.0

Copper binding site 3 out of 4 in 2zmx

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Copper binding site 3 out of 4 in the Crystal Structure of the MET1-Form of the Copper-Bound Tyrosinase in Complex with A Caddie Protein From Streptomyces Castaneoglobisporus Obtained By Soaking in Cupric Sulfate Solution For 36 Hours


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 MET1-Form of the Copper-Bound Tyrosinase in Complex with A Caddie Protein From Streptomyces Castaneoglobisporus Obtained By Soaking in Cupric Sulfate Solution For 36 Hours within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu304

b:29.1
occ:0.50
NE2 A:HIS277 2.0 25.6 1.0
O A:HOH576 2.6 31.7 1.0
O A:HOH729 2.8 30.1 0.5
CE1 A:HIS277 2.9 23.9 1.0
CD2 A:HIS277 3.1 28.6 1.0
ND1 A:HIS277 4.1 22.0 1.0
CG A:HIS277 4.2 27.2 1.0
CG A:PRO231 4.7 21.9 1.0
O A:HOH597 4.7 33.1 1.0

Copper binding site 4 out of 4 in 2zmx

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Copper binding site 4 out of 4 in the Crystal Structure of the MET1-Form of the Copper-Bound Tyrosinase in Complex with A Caddie Protein From Streptomyces Castaneoglobisporus Obtained By Soaking in Cupric Sulfate Solution For 36 Hours


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 MET1-Form of the Copper-Bound Tyrosinase in Complex with A Caddie Protein From Streptomyces Castaneoglobisporus Obtained By Soaking in Cupric Sulfate Solution For 36 Hours within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu303

b:29.8
occ:1.00
ND1 B:HIS68 1.9 30.7 1.0
NE2 B:HIS82 2.0 25.0 1.0
O B:HIS68 2.1 36.8 1.0
N B:HIS68 2.6 35.4 1.0
OE1 B:GLU67 2.6 60.8 1.0
CE1 B:HIS68 2.8 31.4 1.0
C B:HIS68 2.8 40.3 1.0
CD2 B:HIS82 2.9 23.8 1.0
CG B:HIS68 3.0 32.2 1.0
CA B:HIS68 3.0 34.6 1.0
CE1 B:HIS82 3.1 19.7 1.0
CB B:GLU67 3.2 46.4 1.0
C B:GLU67 3.3 40.5 1.0
CB B:HIS68 3.4 31.1 1.0
CD B:GLU67 3.5 50.8 1.0
CA B:GLU67 3.8 45.1 1.0
CG B:GLU67 3.9 48.3 1.0
NE2 B:HIS68 3.9 33.9 1.0
N B:GLY69 4.0 48.0 1.0
CD2 B:HIS68 4.0 33.7 1.0
O B:GLU67 4.1 41.7 1.0
CG B:HIS82 4.1 19.8 1.0
O A:MET43 4.1 18.2 1.0
O B:GLY69 4.1 69.7 1.0
ND1 B:HIS82 4.1 17.6 1.0
C B:GLY69 4.4 58.9 1.0
OE2 B:GLU67 4.6 45.0 1.0
O B:HOH374 4.8 18.4 1.0
CA B:GLY69 4.8 54.5 1.0
N B:GLY70 5.0 56.8 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: Wed Oct 28 14:22:57 2020
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