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Copper in PDB 5z0h: Crystal Structure of Copper-Bound Tyrosinase From Streptomyces Castaneoglobisporus in Complex with the Caddie Protein Obtained By Soaking in the Hydroxylamine-Containing Solution For 2 H at 298 K

Enzymatic activity of Crystal Structure of Copper-Bound Tyrosinase From Streptomyces Castaneoglobisporus in Complex with the Caddie Protein Obtained By Soaking in the Hydroxylamine-Containing Solution For 2 H at 298 K

All present enzymatic activity of Crystal Structure of Copper-Bound Tyrosinase From Streptomyces Castaneoglobisporus in Complex with the Caddie Protein Obtained By Soaking in the Hydroxylamine-Containing Solution For 2 H at 298 K:
1.14.18.1;

Protein crystallography data

The structure of Crystal Structure of Copper-Bound Tyrosinase From Streptomyces Castaneoglobisporus in Complex with the Caddie Protein Obtained By Soaking in the Hydroxylamine-Containing Solution For 2 H at 298 K, PDB code: 5z0h 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 / 1.18
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 64.770, 96.980, 54.550, 90.00, 90.00, 90.00
R / Rfree (%) 13 / 17.1

Copper Binding Sites:

The binding sites of Copper atom in the Crystal Structure of Copper-Bound Tyrosinase From Streptomyces Castaneoglobisporus in Complex with the Caddie Protein Obtained By Soaking in the Hydroxylamine-Containing Solution For 2 H at 298 K (pdb code 5z0h). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 6 binding sites of Copper where determined in the Crystal Structure of Copper-Bound Tyrosinase From Streptomyces Castaneoglobisporus in Complex with the Caddie Protein Obtained By Soaking in the Hydroxylamine-Containing Solution For 2 H at 298 K, PDB code: 5z0h:
Jump to Copper binding site number: 1; 2; 3; 4; 5; 6;

Copper binding site 1 out of 6 in 5z0h

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Copper binding site 1 out of 6 in the Crystal Structure of Copper-Bound Tyrosinase From Streptomyces Castaneoglobisporus in Complex with the Caddie Protein Obtained By Soaking in the Hydroxylamine-Containing Solution For 2 H at 298 K


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 Copper-Bound Tyrosinase From Streptomyces Castaneoglobisporus in Complex with the Caddie Protein Obtained By Soaking in the Hydroxylamine-Containing Solution For 2 H at 298 K within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu301

b:11.3
occ:0.22
CU A:CU301 0.0 11.3 0.2
CU A:CU301 1.1 10.1 0.4
NE2 A:HIS63 1.9 10.7 1.0
NE2 A:HIS38 1.9 9.8 0.6
NE2 A:HIS54 2.1 11.2 0.6
NE2 A:HIS54 2.4 10.7 0.4
O1 A:PER303 2.5 10.3 0.2
CE1 A:HIS63 2.5 9.3 1.0
CD2 A:HIS38 2.6 9.9 0.4
O A:HOH401 2.6 11.2 0.8
CD2 A:HIS38 2.6 10.0 0.6
CE1 A:HIS54 2.6 10.8 0.4
CU A:CU301 2.6 10.3 0.4
NE2 A:HIS38 2.7 9.4 0.4
CE1 A:HIS54 2.9 10.5 0.6
O2 A:PER303 2.9 11.1 0.2
CE1 A:HIS38 3.0 10.0 0.6
CD2 A:HIS63 3.1 9.4 1.0
CD2 A:HIS54 3.3 11.1 0.6
CD2 A:HIS54 3.5 10.1 0.4
ND1 A:HIS54 3.7 10.8 0.4
ND1 A:HIS63 3.8 8.7 1.0
CG A:HIS38 3.8 9.2 0.6
CG A:HIS38 3.9 9.2 0.4
CU A:CU302 3.9 9.3 0.8
ND1 A:HIS38 4.0 9.8 0.6
CE1 A:HIS38 4.0 9.9 0.4
ND1 A:HIS54 4.1 10.5 0.6
CG A:HIS63 4.1 8.6 1.0
OE2 B:DAH98 4.2 12.8 0.6
CZ A:PHE212 4.2 8.8 1.0
CG A:HIS54 4.2 10.2 0.4
CG A:HIS54 4.3 9.9 0.6
CZ3 A:TRP62 4.3 10.1 1.0
NE2 A:HIS216 4.3 9.4 1.0
CE2 A:PHE212 4.4 9.2 1.0
CU A:CU302 4.5 9.8 0.2
ND1 A:HIS38 4.6 8.9 0.4
OZ B:DAH98 4.6 12.1 1.0
CE1 A:HIS216 4.7 9.5 1.0
O A:GLY53 4.8 10.2 1.0
CE3 A:TRP62 4.8 9.0 1.0
CB A:HIS38 5.0 9.6 0.4

Copper binding site 2 out of 6 in 5z0h

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Copper binding site 2 out of 6 in the Crystal Structure of Copper-Bound Tyrosinase From Streptomyces Castaneoglobisporus in Complex with the Caddie Protein Obtained By Soaking in the Hydroxylamine-Containing Solution For 2 H at 298 K


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 Copper-Bound Tyrosinase From Streptomyces Castaneoglobisporus in Complex with the Caddie Protein Obtained By Soaking in the Hydroxylamine-Containing Solution For 2 H at 298 K within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu301

b:10.1
occ:0.36
CU A:CU301 0.0 10.1 0.4
CU A:CU301 1.1 11.3 0.2
CU A:CU301 1.7 10.3 0.4
O A:HOH401 1.8 11.2 0.8
O1 A:PER303 1.9 10.3 0.2
NE2 A:HIS54 1.9 10.7 0.4
NE2 A:HIS54 2.1 11.2 0.6
NE2 A:HIS38 2.1 9.8 0.6
O2 A:PER303 2.1 11.1 0.2
NE2 A:HIS63 2.5 10.7 1.0
NE2 A:HIS38 2.5 9.4 0.4
CE1 A:HIS54 2.6 10.8 0.4
CE1 A:HIS38 2.9 10.0 0.6
CD2 A:HIS54 2.9 11.1 0.6
CD2 A:HIS38 2.9 9.9 0.4
CD2 A:HIS54 3.0 10.1 0.4
OE2 B:DAH98 3.1 12.8 0.6
CE1 A:HIS63 3.1 9.3 1.0
CU A:CU302 3.1 9.3 0.8
CE1 A:HIS54 3.1 10.5 0.6
CD2 A:HIS38 3.2 10.0 0.6
OZ B:DAH98 3.7 12.1 1.0
CD2 A:HIS63 3.7 9.4 1.0
ND1 A:HIS54 3.7 10.8 0.4
CU A:CU302 3.8 9.8 0.2
CE1 A:HIS38 3.8 9.9 0.4
CG A:HIS54 4.0 10.2 0.4
NE2 A:HIS216 4.0 9.4 1.0
ND1 A:HIS38 4.1 9.8 0.6
CG A:HIS54 4.1 9.9 0.6
ND1 A:HIS54 4.2 10.5 0.6
CG A:HIS38 4.3 9.2 0.6
CG A:HIS38 4.3 9.2 0.4
CE2 B:DAH98 4.3 11.4 1.0
CE2 A:PHE212 4.3 9.2 1.0
ND1 A:HIS63 4.4 8.7 1.0
CZ A:PHE212 4.4 8.8 1.0
CE1 A:HIS216 4.5 9.5 1.0
CZ B:DAH98 4.5 10.7 1.0
CD1 A:ILE42 4.6 12.0 0.5
ND1 A:HIS38 4.6 8.9 0.4
NE2 A:HIS190 4.6 8.4 1.0
CG A:HIS63 4.7 8.6 1.0
NE2 A:HIS194 4.8 9.2 1.0
CE1 A:PHE59 4.8 9.0 1.0
CD2 A:HIS216 4.9 9.5 1.0
CG1 A:ILE42 4.9 12.3 0.5

Copper binding site 3 out of 6 in 5z0h

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Copper binding site 3 out of 6 in the Crystal Structure of Copper-Bound Tyrosinase From Streptomyces Castaneoglobisporus in Complex with the Caddie Protein Obtained By Soaking in the Hydroxylamine-Containing Solution For 2 H at 298 K


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 Copper-Bound Tyrosinase From Streptomyces Castaneoglobisporus in Complex with the Caddie Protein Obtained By Soaking in the Hydroxylamine-Containing Solution For 2 H at 298 K within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu301

b:10.3
occ:0.42
CU A:CU301 0.0 10.3 0.4
CU A:CU301 1.7 10.1 0.4
O2 A:PER303 1.9 11.1 0.2
O A:HOH401 2.0 11.2 0.8
OE2 B:DAH98 2.0 12.8 0.6
NE2 A:HIS38 2.1 9.4 0.4
OZ B:DAH98 2.1 12.1 1.0
NE2 A:HIS54 2.1 10.7 0.4
CE1 A:HIS38 2.4 10.0 0.6
NE2 A:HIS38 2.5 9.8 0.6
O1 A:PER303 2.6 10.3 0.2
CU A:CU301 2.6 11.3 0.2
NE2 A:HIS54 2.8 11.2 0.6
CZ B:DAH98 2.9 10.7 1.0
CE2 B:DAH98 3.0 11.4 1.0
CE1 A:HIS38 3.0 9.9 0.4
CE1 A:HIS54 3.1 10.8 0.4
CD2 A:HIS54 3.2 10.1 0.4
CU A:CU302 3.2 9.3 0.8
CD2 A:HIS38 3.2 9.9 0.4
CD2 A:HIS54 3.4 11.1 0.6
CD1 A:ILE42 3.4 12.0 0.5
ND1 A:HIS38 3.7 9.8 0.6
CE1 A:HIS54 3.8 10.5 0.6
CU A:CU302 3.8 9.8 0.2
CD2 A:HIS38 3.8 10.0 0.6
CD1 A:ILE42 3.8 13.4 0.5
CG1 A:ILE42 4.0 12.3 0.5
OG A:SER206 4.1 8.8 1.0
ND1 A:HIS38 4.1 8.9 0.4
NE2 A:HIS63 4.2 10.7 1.0
NE2 A:HIS194 4.2 9.2 1.0
ND1 A:HIS54 4.2 10.8 0.4
CE1 B:DAH98 4.2 10.4 1.0
CD2 B:DAH98 4.3 10.6 1.0
CG A:HIS54 4.3 10.2 0.4
CG A:HIS38 4.3 9.2 0.4
CE1 A:HIS194 4.4 7.9 1.0
CG A:HIS38 4.4 9.2 0.6
CE2 A:PHE212 4.5 9.2 1.0
CG A:HIS54 4.5 9.9 0.6
CG1 A:ILE42 4.5 12.0 0.5
O B:HOH366 4.7 16.1 1.0
ND1 A:HIS54 4.7 10.5 0.6
NE2 A:HIS190 4.7 8.4 1.0
CE1 A:HIS63 4.7 9.3 1.0
NE2 A:HIS216 4.8 9.4 1.0
CE1 A:HIS190 4.9 9.1 1.0
CB A:ILE42 5.0 12.0 0.5

Copper binding site 4 out of 6 in 5z0h

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Copper binding site 4 out of 6 in the Crystal Structure of Copper-Bound Tyrosinase From Streptomyces Castaneoglobisporus in Complex with the Caddie Protein Obtained By Soaking in the Hydroxylamine-Containing Solution For 2 H at 298 K


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 Copper-Bound Tyrosinase From Streptomyces Castaneoglobisporus in Complex with the Caddie Protein Obtained By Soaking in the Hydroxylamine-Containing Solution For 2 H at 298 K within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu302

b:9.8
occ:0.22
CU A:CU302 0.0 9.8 0.2
CU A:CU302 0.9 9.3 0.8
NE2 A:HIS194 1.7 9.2 1.0
NE2 A:HIS216 1.9 9.4 1.0
O1 A:PER303 2.1 10.3 0.2
O A:HOH401 2.1 11.2 0.8
NE2 A:HIS190 2.3 8.4 1.0
O2 A:PER303 2.3 11.1 0.2
CE1 A:HIS194 2.7 7.9 1.0
CD2 A:HIS216 2.7 9.5 1.0
CD2 A:HIS194 2.9 9.3 1.0
CD2 A:HIS190 3.0 8.6 1.0
CE1 A:HIS216 3.1 9.5 1.0
CE1 A:HIS190 3.4 9.1 1.0
OE2 B:DAH98 3.4 12.8 0.6
CU A:CU301 3.8 10.1 0.4
CU A:CU301 3.8 10.3 0.4
ND1 A:HIS194 3.8 8.0 1.0
CG A:HIS216 3.9 8.8 1.0
CG A:HIS194 4.0 7.5 1.0
CD2 A:HIS215 4.0 10.1 1.0
CE2 A:PHE212 4.0 9.2 1.0
CE2 B:DAH98 4.0 11.4 1.0
ND1 A:HIS216 4.1 8.9 1.0
OZ B:DAH98 4.2 12.1 1.0
CG A:HIS190 4.3 8.4 1.0
NE2 A:HIS215 4.3 10.2 1.0
CZ B:DAH98 4.4 10.7 1.0
ND1 A:HIS190 4.4 9.1 1.0
CU A:CU301 4.5 11.3 0.2
CD2 A:PHE212 4.6 8.1 1.0
NE2 A:HIS63 4.7 10.7 1.0
CZ A:PHE212 4.7 8.8 1.0
CD2 B:DAH98 4.9 10.6 1.0

Copper binding site 5 out of 6 in 5z0h

Go back to Copper Binding Sites List in 5z0h
Copper binding site 5 out of 6 in the Crystal Structure of Copper-Bound Tyrosinase From Streptomyces Castaneoglobisporus in Complex with the Caddie Protein Obtained By Soaking in the Hydroxylamine-Containing Solution For 2 H at 298 K


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 Copper-Bound Tyrosinase From Streptomyces Castaneoglobisporus in Complex with the Caddie Protein Obtained By Soaking in the Hydroxylamine-Containing Solution For 2 H at 298 K within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu302

b:9.3
occ:0.78
CU A:CU302 0.0 9.3 0.8
CU A:CU302 0.9 9.8 0.2
O1 A:PER303 1.6 10.3 0.2
O A:HOH401 1.7 11.2 0.8
NE2 A:HIS190 2.0 8.4 1.0
O2 A:PER303 2.0 11.1 0.2
NE2 A:HIS216 2.2 9.4 1.0
NE2 A:HIS194 2.2 9.2 1.0
OE2 B:DAH98 2.8 12.8 0.6
CE1 A:HIS190 2.9 9.1 1.0
CE1 A:HIS216 3.1 9.5 1.0
CD2 A:HIS190 3.1 8.6 1.0
CU A:CU301 3.1 10.1 0.4
CE1 A:HIS194 3.2 7.9 1.0
CU A:CU301 3.2 10.3 0.4
CD2 A:HIS194 3.2 9.3 1.0
CD2 A:HIS216 3.2 9.5 1.0
CE2 B:DAH98 3.6 11.4 1.0
OZ B:DAH98 3.9 12.1 1.0
CU A:CU301 3.9 11.3 0.2
CZ B:DAH98 4.1 10.7 1.0
ND1 A:HIS190 4.1 9.1 1.0
NE2 A:HIS63 4.2 10.7 1.0
CG A:HIS190 4.2 8.4 1.0
ND1 A:HIS216 4.2 8.9 1.0
ND1 A:HIS194 4.3 8.0 1.0
CG A:HIS194 4.3 7.5 1.0
NE2 A:HIS54 4.3 10.7 0.4
CG A:HIS216 4.3 8.8 1.0
CE2 A:PHE212 4.4 9.2 1.0
CD2 B:DAH98 4.5 10.6 1.0
CE1 A:PHE59 4.5 9.0 1.0
NE2 A:HIS38 4.7 9.8 0.6
CD2 A:HIS54 4.7 10.1 0.4
NE2 A:HIS38 4.8 9.4 0.4
CD2 A:HIS63 4.8 9.4 1.0
NE2 A:HIS54 4.8 11.2 0.6
CE1 A:HIS63 4.8 9.3 1.0
CD2 A:HIS215 4.8 10.1 1.0
CZ A:PHE59 4.9 9.8 1.0
CD2 A:HIS54 4.9 11.1 0.6
CZ A:PHE212 4.9 8.8 1.0
NE2 A:HIS215 4.9 10.2 1.0

Copper binding site 6 out of 6 in 5z0h

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Copper binding site 6 out of 6 in the Crystal Structure of Copper-Bound Tyrosinase From Streptomyces Castaneoglobisporus in Complex with the Caddie Protein Obtained By Soaking in the Hydroxylamine-Containing Solution For 2 H at 298 K


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 6 of Crystal Structure of Copper-Bound Tyrosinase From Streptomyces Castaneoglobisporus in Complex with the Caddie Protein Obtained By Soaking in the Hydroxylamine-Containing Solution For 2 H at 298 K within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu201

b:16.8
occ:1.00
NE2 B:HIS97 2.0 15.2 1.0
NE2 B:HIS82 2.0 15.6 1.0
SD B:MET84 2.2 18.9 1.0
CE1 B:HIS97 2.9 14.5 1.0
CE1 B:HIS82 3.0 16.1 1.0
CD2 B:HIS82 3.0 15.6 1.0
CD2 B:HIS97 3.1 15.9 1.0
CG B:MET84 3.2 18.1 1.0
O A:ILE42 3.2 13.6 1.0
CE B:MET84 3.2 19.7 1.0
CB B:MET84 3.5 15.3 1.0
CA A:MET43 3.9 14.3 1.0
ND1 B:HIS97 4.0 14.2 1.0
ND1 B:HIS82 4.1 15.9 1.0
C A:ILE42 4.1 12.3 1.0
CG B:HIS82 4.2 14.4 1.0
CG B:HIS97 4.2 12.5 1.0
O A:MET43 4.2 23.8 1.0
C A:MET43 4.4 14.6 1.0
N A:MET43 4.5 12.1 1.0
CG2 A:ILE42 4.5 13.0 0.5
O A:HOH429 4.6 16.3 1.0
CA B:MET84 4.7 11.8 1.0
N B:MET84 4.8 11.4 1.0
CG1 B:ILE92 4.8 13.8 1.0
C B:VAL83 4.9 11.6 1.0
CB A:MET43 4.9 16.1 1.0
O B:VAL83 4.9 14.8 1.0
CG A:MET43 5.0 18.2 1.0

Reference:

Y.Matoba, M.Sugiyama. Catalytic Mechanism of Tyrosinase Implied From the Quinone Formation on the TYR98 Residue of the Caddie Protein To Be Published.
Page generated: Sun Dec 13 11:20:39 2020

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