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Copper in PDB 2zmz: The 1.37-A Crystal Structure of the Hydroxylamine-Induced Deoxy-Form of the Copper-Bound Tyrosinase in Complex with A Caddie Protein From Streptomyces Castaneoglobisporus

Enzymatic activity of The 1.37-A Crystal Structure of the Hydroxylamine-Induced Deoxy-Form of the Copper-Bound Tyrosinase in Complex with A Caddie Protein From Streptomyces Castaneoglobisporus

All present enzymatic activity of The 1.37-A Crystal Structure of the Hydroxylamine-Induced Deoxy-Form of the Copper-Bound Tyrosinase in Complex with A Caddie Protein From Streptomyces Castaneoglobisporus:
1.14.18.1;

Protein crystallography data

The structure of The 1.37-A Crystal Structure of the Hydroxylamine-Induced Deoxy-Form of the Copper-Bound Tyrosinase in Complex with A Caddie Protein From Streptomyces Castaneoglobisporus, PDB code: 2zmz 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 / 1.37
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 65.180, 98.030, 55.200, 90.00, 90.00, 90.00
R / Rfree (%) 18.6 / 23.2

Copper Binding Sites:

The binding sites of Copper atom in the The 1.37-A Crystal Structure of the Hydroxylamine-Induced Deoxy-Form of the Copper-Bound Tyrosinase in Complex with A Caddie Protein From Streptomyces Castaneoglobisporus (pdb code 2zmz). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 4 binding sites of Copper where determined in the The 1.37-A Crystal Structure of the Hydroxylamine-Induced Deoxy-Form of the Copper-Bound Tyrosinase in Complex with A Caddie Protein From Streptomyces Castaneoglobisporus, PDB code: 2zmz:
Jump to Copper binding site number: 1; 2; 3; 4;

Copper binding site 1 out of 4 in 2zmz

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Copper binding site 1 out of 4 in the The 1.37-A Crystal Structure of the Hydroxylamine-Induced Deoxy-Form of the Copper-Bound Tyrosinase in Complex with A Caddie Protein From Streptomyces Castaneoglobisporus


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of The 1.37-A Crystal Structure of the Hydroxylamine-Induced Deoxy-Form of the Copper-Bound Tyrosinase in Complex with A Caddie Protein From Streptomyces Castaneoglobisporus within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu301

b:32.0
occ:1.00
 NE2 A:HIS38 1.9 15.9 1.0
NE2 A:HIS54 2.1 19.5 1.0
NE2 A:HIS63 2.2 11.0 1.0
O B:HOH340 2.4 14.7 1.0
CD2 A:HIS38 2.8 16.4 1.0
CE1 A:HIS38 2.9 17.2 1.0
CE1 A:HIS63 2.9 9.4 1.0
CD2 A:HIS54 3.0 19.5 1.0
CE1 A:HIS54 3.2 19.0 1.0
CD2 A:HIS63 3.4 9.1 1.0
CG A:HIS38 3.9 12.6 1.0
ND1 A:HIS38 3.9 13.5 1.0
CU A:CU1302 4.1 16.4 1.0
CZ A:PHE212 4.1 7.4 1.0
ND1 A:HIS63 4.1 8.9 1.0
CG A:HIS54 4.2 17.1 1.0
NE2 A:HIS216 4.2 10.8 1.0
ND1 A:HIS54 4.3 14.8 1.0
CE2 A:PHE212 4.3 10.6 1.0
OH B:TYR98 4.4 20.9 1.0
CG A:HIS63 4.4 8.3 1.0
CE1 A:HIS216 4.5 11.5 1.0
CZ3 A:TRP62 4.7 13.0 1.0
O A:GLY53 5.0 11.7 1.0

Copper binding site 2 out of 4 in 2zmz

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Copper binding site 2 out of 4 in the The 1.37-A Crystal Structure of the Hydroxylamine-Induced Deoxy-Form of the Copper-Bound Tyrosinase in Complex with A Caddie Protein From Streptomyces Castaneoglobisporus


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of The 1.37-A Crystal Structure of the Hydroxylamine-Induced Deoxy-Form of the Copper-Bound Tyrosinase in Complex with A Caddie Protein From Streptomyces Castaneoglobisporus within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu302

b:16.4
occ:1.00
 NE2 A:HIS194 2.0 9.2 1.0
NE2 A:HIS216 2.0 10.8 1.0
NE2 A:HIS190 2.0 8.5 1.0
O B:HOH340 2.0 14.7 1.0
CE1 A:HIS216 2.9 11.5 1.0
CE1 A:HIS194 3.0 9.2 1.0
CD2 A:HIS190 3.0 10.4 1.0
CE1 A:HIS190 3.0 9.3 1.0
CD2 A:HIS194 3.1 10.0 1.0
CD2 A:HIS216 3.1 10.5 1.0
ND1 A:HIS216 4.1 10.0 1.0
CE2 A:PHE212 4.1 10.6 1.0
CU A:CU1301 4.1 32.0 1.0
OH B:TYR98 4.1 20.9 1.0
ND1 A:HIS190 4.1 9.7 1.0
ND1 A:HIS194 4.1 8.9 1.0
CG A:HIS190 4.1 8.3 1.0
CE2 B:TYR98 4.1 14.0 1.0
CG A:HIS194 4.2 8.7 1.0
CG A:HIS216 4.2 10.5 1.0
CD2 A:HIS215 4.3 10.7 1.0
CZ B:TYR98 4.4 14.1 1.0
NE2 A:HIS215 4.5 11.8 1.0
NE2 A:HIS63 4.7 11.0 1.0
CZ A:PHE212 4.7 7.4 1.0
CD2 A:PHE212 4.8 8.3 1.0
CE1 A:PHE59 4.9 8.1 1.0

Copper binding site 3 out of 4 in 2zmz

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Copper binding site 3 out of 4 in the The 1.37-A Crystal Structure of the Hydroxylamine-Induced Deoxy-Form of the Copper-Bound Tyrosinase in Complex with A Caddie Protein From Streptomyces Castaneoglobisporus


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 3 of The 1.37-A Crystal Structure of the Hydroxylamine-Induced Deoxy-Form of the Copper-Bound Tyrosinase in Complex with A Caddie Protein From Streptomyces Castaneoglobisporus within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu303

b:24.5
occ:0.63
 NE2 B:HIS82 2.0 16.3 0.6
NE2 B:HIS97 2.3 22.1 0.6
SD B:MET84 2.4 36.1 1.0
O3 B:NO3304 2.5 18.2 0.4
N B:NO3304 2.6 19.0 0.4
CE1 B:HIS97 2.8 22.7 0.4
CE1 B:HIS97 2.9 22.4 0.6
NE2 B:HIS97 3.0 22.3 0.4
O2 B:NO3304 3.0 19.6 0.4
CE1 B:HIS82 3.0 16.6 0.6
O1 B:NO3304 3.0 30.4 0.4
CD2 B:HIS82 3.1 16.1 0.6
CG B:MET84 3.3 26.9 1.0
CE B:MET84 3.3 25.5 1.0
O A:ILE42 3.3 16.9 1.0
CB B:MET84 3.5 17.2 1.0
CD2 B:HIS97 3.5 19.5 0.6
ND1 B:HIS82 3.6 14.8 0.4
CE1 B:HIS82 3.6 14.8 0.4
CA A:MET43 3.8 15.2 1.0
ND1 B:HIS97 3.9 21.1 0.4
O A:MET43 4.0 21.5 1.0
ND1 B:HIS82 4.1 15.6 0.6
ND1 B:HIS97 4.1 19.2 0.6
CD2 B:HIS97 4.2 20.1 0.4
CG B:HIS82 4.2 14.0 0.6
C A:MET43 4.2 14.7 1.0
C A:ILE42 4.3 16.7 1.0
CG B:HIS97 4.5 18.7 0.6
N A:MET43 4.5 14.1 1.0
O A:HOH412 4.6 21.5 1.0
CA B:MET84 4.7 14.2 1.0
CG B:HIS97 4.7 18.8 0.4
N B:MET84 4.7 13.6 1.0
CD1 B:ILE92 4.8 22.5 1.0
CB A:MET43 4.8 17.7 1.0
CG1 B:ILE92 4.8 14.1 1.0
CG A:MET43 4.9 20.6 1.0
NE2 B:HIS82 4.9 15.8 0.4
CG B:HIS82 4.9 14.1 0.4
C B:VAL83 4.9 12.1 1.0

Copper binding site 4 out of 4 in 2zmz

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Copper binding site 4 out of 4 in the The 1.37-A Crystal Structure of the Hydroxylamine-Induced Deoxy-Form of the Copper-Bound Tyrosinase in Complex with A Caddie Protein From Streptomyces Castaneoglobisporus


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 4 of The 1.37-A Crystal Structure of the Hydroxylamine-Induced Deoxy-Form of the Copper-Bound Tyrosinase in Complex with A Caddie Protein From Streptomyces Castaneoglobisporus within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu303

b:18.1
occ:0.37
 ND1 B:HIS68 1.7 86.8 1.0
NE2 B:HIS82 2.0 15.8 0.4
CE1 B:HIS68 2.1 87.2 1.0
CB B:GLU67 2.2 66.5 1.0
OE1 B:GLU67 2.3 55.5 1.0
N B:HIS68 2.8 79.0 1.0
CG B:GLU67 2.8 61.1 1.0
CD2 B:HIS82 2.9 15.1 0.4
CD B:GLU67 2.9 56.4 1.0
CG B:HIS68 3.0 86.4 1.0
CE1 B:HIS82 3.0 14.8 0.4
NE2 B:HIS68 3.4 87.5 1.0
CA B:GLU67 3.4 71.9 1.0
ND1 B:HIS82 3.4 15.6 0.6
CE1 B:HIS82 3.6 16.6 0.6
C B:GLU67 3.6 74.4 1.0
CA B:HIS68 3.7 82.5 1.0
CD2 B:HIS68 3.8 87.2 1.0
CB B:HIS68 3.8 84.4 1.0
CG B:HIS82 4.1 14.1 0.4
C B:HIS68 4.1 83.6 1.0
ND1 B:HIS82 4.1 14.8 0.4
OE2 B:GLU67 4.1 45.1 1.0
O B:HIS68 4.1 89.4 1.0
O A:MET43 4.2 21.5 1.0
N B:GLU67 4.5 75.0 1.0
O B:HOH424 4.7 21.9 1.0
CG B:HIS82 4.8 14.0 0.6
O B:GLU67 4.8 70.3 1.0
O B:GLY69 4.8 81.8 1.0
N B:GLY69 4.9 81.6 1.0
NE2 B:HIS82 4.9 16.3 0.6
C B:GLY69 5.0 76.6 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: Wed Jul 31 00:29:39 2024

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