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Copper in PDB 2zmy: Crystal Structure of the MET2-Form of the Copper-Bound Tyrosinase in Complex with A Caddie Protein From Streptomyces Castaneoglobisporus Obtained By Soaking in Cupric Sulfate Solution For 80 Hours

Enzymatic activity of Crystal Structure of the MET2-Form of the Copper-Bound Tyrosinase in Complex with A Caddie Protein From Streptomyces Castaneoglobisporus Obtained By Soaking in Cupric Sulfate Solution For 80 Hours

All present enzymatic activity of Crystal Structure of the MET2-Form of the Copper-Bound Tyrosinase in Complex with A Caddie Protein From Streptomyces Castaneoglobisporus Obtained By Soaking in Cupric Sulfate Solution For 80 Hours:
1.14.18.1;

Protein crystallography data

The structure of Crystal Structure of the MET2-Form of the Copper-Bound Tyrosinase in Complex with A Caddie Protein From Streptomyces Castaneoglobisporus Obtained By Soaking in Cupric Sulfate Solution For 80 Hours, PDB code: 2zmy 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 / 1.45
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 64.740, 97.550, 54.970, 90.00, 90.00, 90.00
R / Rfree (%) 16.9 / 21.4

Copper Binding Sites:

The binding sites of Copper atom in the Crystal Structure of the MET2-Form of the Copper-Bound Tyrosinase in Complex with A Caddie Protein From Streptomyces Castaneoglobisporus Obtained By Soaking in Cupric Sulfate Solution For 80 Hours (pdb code 2zmy). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 5 binding sites of Copper where determined in the Crystal Structure of the MET2-Form of the Copper-Bound Tyrosinase in Complex with A Caddie Protein From Streptomyces Castaneoglobisporus Obtained By Soaking in Cupric Sulfate Solution For 80 Hours, PDB code: 2zmy:
Jump to Copper binding site number: 1; 2; 3; 4; 5;

Copper binding site 1 out of 5 in 2zmy

Go back to Copper Binding Sites List in 2zmy
Copper binding site 1 out of 5 in the Crystal Structure of the MET2-Form of the Copper-Bound Tyrosinase in Complex with A Caddie Protein From Streptomyces Castaneoglobisporus Obtained By Soaking in Cupric Sulfate Solution For 80 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 MET2-Form of the Copper-Bound Tyrosinase in Complex with A Caddie Protein From Streptomyces Castaneoglobisporus Obtained By Soaking in Cupric Sulfate Solution For 80 Hours within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu301

b:84.8
occ:1.00
NE2 A:HIS180 2.0 14.5 1.0
O A:HOH678 2.6 56.7 1.0
CE1 A:HIS180 2.9 18.5 1.0
CD2 A:HIS180 3.0 14.0 1.0
OE2 A:GLU175 3.4 41.2 1.0
CA A:GLY186 3.8 11.9 1.0
O A:HOH471 3.9 23.9 1.0
OE1 A:GLU175 4.0 46.5 1.0
ND1 A:HIS180 4.1 14.3 1.0
CG A:HIS180 4.1 11.7 1.0
CD A:GLU175 4.1 30.7 1.0
N A:GLY186 4.1 13.9 1.0
O A:HOH613 4.3 36.6 1.0
C A:ARG185 4.6 13.2 1.0
CB A:ARG185 4.8 14.7 1.0
O A:ARG185 4.8 13.4 1.0
O A:HOH464 4.9 23.6 1.0
O A:HOH681 5.0 57.5 1.0

Copper binding site 2 out of 5 in 2zmy

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Copper binding site 2 out of 5 in the Crystal Structure of the MET2-Form of the Copper-Bound Tyrosinase in Complex with A Caddie Protein From Streptomyces Castaneoglobisporus Obtained By Soaking in Cupric Sulfate Solution For 80 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 MET2-Form of the Copper-Bound Tyrosinase in Complex with A Caddie Protein From Streptomyces Castaneoglobisporus Obtained By Soaking in Cupric Sulfate Solution For 80 Hours within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu302

b:36.4
occ:1.00
O A:HOH306 2.0 19.6 1.0
O A:HOH307 2.0 16.5 1.0
NE2 A:HIS38 2.2 20.5 1.0
NE2 A:HIS54 2.2 13.3 0.5
CE1 A:HIS38 2.6 16.8 1.0
CD2 A:HIS54 2.8 14.1 0.5
NE2 A:HIS63 2.8 12.0 1.0
CU A:CU303 3.1 17.9 1.0
CE1 A:HIS63 3.3 12.5 1.0
CE1 A:HIS54 3.4 14.2 0.5
CD2 A:HIS38 3.5 19.6 1.0
OH B:TYR98 3.7 23.8 1.0
ND1 A:HIS38 3.9 16.3 1.0
CD2 A:HIS63 4.0 10.1 1.0
NE2 A:HIS216 4.0 13.3 1.0
CG A:HIS54 4.1 12.7 0.5
CD1 A:ILE42 4.2 31.9 1.0
CG A:HIS38 4.3 15.3 1.0
ND1 A:HIS54 4.3 12.5 0.5
CG1 A:ILE42 4.4 24.0 1.0
CE1 A:HIS216 4.4 12.9 1.0
CE2 A:PHE212 4.4 8.6 1.0
CZ A:PHE212 4.5 9.0 1.0
ND1 A:HIS63 4.6 10.0 1.0
NE2 A:HIS190 4.6 10.5 1.0
NE2 A:HIS194 4.7 9.4 1.0
CZ B:TYR98 4.7 16.7 1.0
CE2 B:TYR98 4.8 18.6 1.0
CE1 A:PHE59 4.9 9.3 1.0
CG A:HIS63 4.9 8.6 1.0
CE1 A:HIS190 5.0 11.5 1.0

Copper binding site 3 out of 5 in 2zmy

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Copper binding site 3 out of 5 in the Crystal Structure of the MET2-Form of the Copper-Bound Tyrosinase in Complex with A Caddie Protein From Streptomyces Castaneoglobisporus Obtained By Soaking in Cupric Sulfate Solution For 80 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 MET2-Form of the Copper-Bound Tyrosinase in Complex with A Caddie Protein From Streptomyces Castaneoglobisporus Obtained By Soaking in Cupric Sulfate Solution For 80 Hours within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu303

b:17.9
occ:1.00
O A:HOH307 1.9 16.5 1.0
NE2 A:HIS190 2.0 10.5 1.0
NE2 A:HIS194 2.1 9.4 1.0
NE2 A:HIS216 2.3 13.3 1.0
O A:HOH306 2.3 19.6 1.0
CE1 A:HIS190 2.9 11.5 1.0
CE1 A:HIS216 3.0 12.9 1.0
CE1 A:HIS194 3.1 9.8 1.0
CD2 A:HIS190 3.1 10.6 1.0
CU A:CU302 3.1 36.4 1.0
CD2 A:HIS194 3.1 9.0 1.0
CD2 A:HIS216 3.4 10.3 1.0
OH B:TYR98 4.0 23.8 1.0
ND1 A:HIS190 4.1 9.4 1.0
CE2 B:TYR98 4.1 18.6 1.0
CG A:HIS190 4.2 7.0 1.0
ND1 A:HIS216 4.2 9.9 1.0
ND1 A:HIS194 4.2 8.5 1.0
CG A:HIS194 4.3 9.3 1.0
CZ B:TYR98 4.3 16.7 1.0
CE2 A:PHE212 4.4 8.6 1.0
CG A:HIS216 4.4 9.5 1.0
NE2 A:HIS63 4.5 12.0 1.0
CD2 A:HIS215 4.7 12.9 1.0
CE1 A:PHE59 4.7 9.3 1.0
NE2 A:HIS215 4.7 13.5 1.0
NE2 A:HIS38 4.8 20.5 1.0
CE1 A:HIS38 4.9 16.8 1.0
CZ A:PHE212 5.0 9.0 1.0

Copper binding site 4 out of 5 in 2zmy

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Copper binding site 4 out of 5 in the Crystal Structure of the MET2-Form of the Copper-Bound Tyrosinase in Complex with A Caddie Protein From Streptomyces Castaneoglobisporus Obtained By Soaking in Cupric Sulfate Solution For 80 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 MET2-Form of the Copper-Bound Tyrosinase in Complex with A Caddie Protein From Streptomyces Castaneoglobisporus Obtained By Soaking in Cupric Sulfate Solution For 80 Hours within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu305

b:39.2
occ:0.50
NE2 A:HIS277 1.8 65.6 1.0
O A:HOH686 2.3 24.1 0.5
CE1 A:HIS277 2.8 66.4 1.0
CD2 A:HIS277 2.9 66.3 1.0
ND1 A:HIS277 3.9 66.8 1.0
CG A:HIS277 4.0 66.8 1.0
CG A:PRO231 4.7 24.1 1.0

Copper binding site 5 out of 5 in 2zmy

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Copper binding site 5 out of 5 in the Crystal Structure of the MET2-Form of the Copper-Bound Tyrosinase in Complex with A Caddie Protein From Streptomyces Castaneoglobisporus Obtained By Soaking in Cupric Sulfate Solution For 80 Hours


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 5 of Crystal Structure of the MET2-Form of the Copper-Bound Tyrosinase in Complex with A Caddie Protein From Streptomyces Castaneoglobisporus Obtained By Soaking in Cupric Sulfate Solution For 80 Hours within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu304

b:22.9
occ:1.00
OE1 B:GLU67 1.9 29.6 1.0
NE2 B:HIS82 2.0 17.6 1.0
O B:HIS68 2.0 26.2 1.0
ND1 B:HIS68 2.1 20.6 1.0
N B:HIS68 2.6 21.3 1.0
C B:HIS68 2.8 26.5 1.0
O B:HOH558 2.9 31.1 1.0
CE1 B:HIS68 2.9 20.3 1.0
CD2 B:HIS82 3.0 18.3 1.0
CE1 B:HIS82 3.0 15.3 1.0
CA B:HIS68 3.1 20.7 1.0
CD B:GLU67 3.1 32.8 1.0
CG B:HIS68 3.2 20.5 1.0
C B:GLU67 3.2 24.3 1.0
CB B:GLU67 3.5 26.2 1.0
CB B:HIS68 3.6 18.5 1.0
O B:GLU67 3.9 26.8 1.0
CA B:GLU67 3.9 25.7 1.0
CG B:GLU67 3.9 29.4 1.0
N B:GLY69 4.0 33.1 1.0
OE2 B:GLU67 4.0 30.2 1.0
NE2 B:HIS68 4.1 19.0 1.0
ND1 B:HIS82 4.1 14.0 1.0
CG B:HIS82 4.1 15.1 1.0
O A:MET43 4.1 16.6 1.0
CD2 B:HIS68 4.2 19.7 1.0
N B:GLY70 4.3 48.2 1.0
CA B:GLY69 4.7 42.3 1.0
O B:HOH405 4.8 19.5 1.0
CA B:GLY70 4.8 45.8 1.0
C B:GLY69 4.9 49.0 1.0

Reference:

Y.Matoba, H.Yoshitsu, H.-J.Jeon, K.Oda, M.Noda, T.Kumagai, M.Sugiyama. X-Ray Snapshots of A Hydroxylation Mechanism of Tyrosinase To Be Published.
Page generated: Sun Dec 13 11:08:27 2020

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