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Copper in PDB 5z0m: Crystal Structure of Copper-Bound H63F-Mutated Tyrosinase From Streptomyces Castaneoglobisporus in Complex with the Caddie Protein Obtained By Soaking in the Hydroxylamine-Containing Solution For 12 H at 298 K

Enzymatic activity of Crystal Structure of Copper-Bound H63F-Mutated Tyrosinase From Streptomyces Castaneoglobisporus in Complex with the Caddie Protein Obtained By Soaking in the Hydroxylamine-Containing Solution For 12 H at 298 K

All present enzymatic activity of Crystal Structure of Copper-Bound H63F-Mutated Tyrosinase From Streptomyces Castaneoglobisporus in Complex with the Caddie Protein Obtained By Soaking in the Hydroxylamine-Containing Solution For 12 H at 298 K:
1.14.18.1;

Protein crystallography data

The structure of Crystal Structure of Copper-Bound H63F-Mutated Tyrosinase From Streptomyces Castaneoglobisporus in Complex with the Caddie Protein Obtained By Soaking in the Hydroxylamine-Containing Solution For 12 H at 298 K, PDB code: 5z0m 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 / 1.70
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 64.910, 97.350, 54.920, 90.00, 90.00, 90.00
R / Rfree (%) 14.2 / 20.7

Copper Binding Sites:

The binding sites of Copper atom in the Crystal Structure of Copper-Bound H63F-Mutated Tyrosinase From Streptomyces Castaneoglobisporus in Complex with the Caddie Protein Obtained By Soaking in the Hydroxylamine-Containing Solution For 12 H at 298 K (pdb code 5z0m). 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 Copper-Bound H63F-Mutated Tyrosinase From Streptomyces Castaneoglobisporus in Complex with the Caddie Protein Obtained By Soaking in the Hydroxylamine-Containing Solution For 12 H at 298 K, PDB code: 5z0m:
Jump to Copper binding site number: 1; 2; 3; 4; 5;

Copper binding site 1 out of 5 in 5z0m

Go back to Copper Binding Sites List in 5z0m
Copper binding site 1 out of 5 in the Crystal Structure of Copper-Bound H63F-Mutated Tyrosinase From Streptomyces Castaneoglobisporus in Complex with the Caddie Protein Obtained By Soaking in the Hydroxylamine-Containing Solution For 12 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 H63F-Mutated Tyrosinase From Streptomyces Castaneoglobisporus in Complex with the Caddie Protein Obtained By Soaking in the Hydroxylamine-Containing Solution For 12 H at 298 K within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu301

b:42.1
occ:0.94
 O B:HOH351 1.8 27.2 1.0
OE2 B:DAH98 2.1 16.6 0.3
NE2 A:HIS38 2.2 19.2 1.0
NE2 A:HIS54 2.5 37.2 1.0
OZ B:DAH98 2.5 15.7 1.0
CE1 A:HIS38 3.0 18.5 1.0
CD2 A:HIS54 3.1 35.6 1.0
CU A:CU302 3.2 16.1 0.5
CE2 B:DAH98 3.2 17.5 1.0
CD2 A:HIS38 3.3 18.7 1.0
CD1 A:ILE42 3.3 36.4 1.0
CZ B:DAH98 3.4 17.4 1.0
CU A:CU302 3.6 19.0 0.5
CE1 A:HIS54 3.6 37.0 1.0
CZ A:PHE63 4.0 17.8 1.0
NE2 A:HIS194 4.2 13.9 1.0
ND1 A:HIS38 4.2 18.5 1.0
OG A:SER206 4.3 17.0 1.0
CE2 A:PHE212 4.3 15.0 1.0
CG A:HIS38 4.4 18.1 1.0
CG A:HIS54 4.4 33.8 1.0
CE1 A:HIS194 4.4 13.5 1.0
CG1 A:ILE42 4.5 32.7 1.0
CD2 B:DAH98 4.5 18.2 1.0
NE2 A:HIS190 4.6 15.0 1.0
NE2 A:HIS216 4.6 14.5 1.0
CE1 B:DAH98 4.6 16.7 1.0
ND1 A:HIS54 4.6 35.4 1.0
O B:HOH364 4.7 37.7 1.0
CE1 A:PHE63 4.7 17.3 1.0
CE1 A:HIS190 4.7 14.8 1.0
CZ A:PHE212 4.8 15.5 1.0
CE2 A:PHE63 4.8 17.7 1.0

Copper binding site 2 out of 5 in 5z0m

Go back to Copper Binding Sites List in 5z0m
Copper binding site 2 out of 5 in the Crystal Structure of Copper-Bound H63F-Mutated Tyrosinase From Streptomyces Castaneoglobisporus in Complex with the Caddie Protein Obtained By Soaking in the Hydroxylamine-Containing Solution For 12 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 H63F-Mutated Tyrosinase From Streptomyces Castaneoglobisporus in Complex with the Caddie Protein Obtained By Soaking in the Hydroxylamine-Containing Solution For 12 H at 298 K within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu302

b:19.0
occ:0.54
 CU A:CU302 0.0 19.0 0.5
CU A:CU302 0.7 16.1 0.5
NE2 A:HIS194 1.8 13.9 1.0
NE2 A:HIS216 2.1 14.5 1.0
NE2 A:HIS190 2.1 15.0 1.0
O B:HOH351 2.2 27.2 1.0
CE1 A:HIS194 2.8 13.5 1.0
CD2 A:HIS194 2.8 14.5 1.0
CD2 A:HIS190 2.9 14.8 1.0
CD2 A:HIS216 3.0 13.8 1.0
CE1 A:HIS216 3.1 14.2 1.0
CE1 A:HIS190 3.2 14.8 1.0
OE2 B:DAH98 3.4 16.6 0.3
CU A:CU301 3.6 42.1 0.9
ND1 A:HIS194 3.9 13.1 1.0
CG A:HIS194 3.9 14.4 1.0
CD2 A:HIS215 4.0 13.5 1.0
CG A:HIS190 4.1 14.6 1.0
CE2 A:PHE212 4.1 15.0 1.0
CG A:HIS216 4.2 13.4 1.0
NE2 A:HIS215 4.2 13.2 1.0
ND1 A:HIS216 4.2 13.9 1.0
ND1 A:HIS190 4.2 14.9 1.0
CE2 B:DAH98 4.2 17.5 1.0
OZ B:DAH98 4.4 15.7 1.0
CZ B:DAH98 4.5 17.4 1.0
CD2 A:PHE212 4.7 14.3 1.0
CZ A:PHE212 4.7 15.5 1.0
CZ A:PHE63 4.8 17.8 1.0
CD2 B:DAH98 5.0 18.2 1.0

Copper binding site 3 out of 5 in 5z0m

Go back to Copper Binding Sites List in 5z0m
Copper binding site 3 out of 5 in the Crystal Structure of Copper-Bound H63F-Mutated Tyrosinase From Streptomyces Castaneoglobisporus in Complex with the Caddie Protein Obtained By Soaking in the Hydroxylamine-Containing Solution For 12 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 H63F-Mutated Tyrosinase From Streptomyces Castaneoglobisporus in Complex with the Caddie Protein Obtained By Soaking in the Hydroxylamine-Containing Solution For 12 H at 298 K within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu302

b:16.1
occ:0.46
 CU A:CU302 0.0 16.1 0.5
CU A:CU302 0.7 19.0 0.5
NE2 A:HIS190 1.9 15.0 1.0
O B:HOH351 1.9 27.2 1.0
NE2 A:HIS216 2.1 14.5 1.0
NE2 A:HIS194 2.3 13.9 1.0
CE1 A:HIS190 2.8 14.8 1.0
CD2 A:HIS190 2.9 14.8 1.0
CE1 A:HIS216 2.9 14.2 1.0
OE2 B:DAH98 3.0 16.6 0.3
CU A:CU301 3.2 42.1 0.9
CD2 A:HIS194 3.2 14.5 1.0
CD2 A:HIS216 3.3 13.8 1.0
CE1 A:HIS194 3.3 13.5 1.0
ND1 A:HIS190 4.0 14.9 1.0
CE2 B:DAH98 4.0 17.5 1.0
CG A:HIS190 4.1 14.6 1.0
ND1 A:HIS216 4.1 13.9 1.0
OZ B:DAH98 4.3 15.7 1.0
CG A:HIS216 4.3 13.4 1.0
CZ A:PHE63 4.3 17.8 1.0
CE2 A:PHE212 4.4 15.0 1.0
CG A:HIS194 4.4 14.4 1.0
ND1 A:HIS194 4.4 13.1 1.0
CZ B:DAH98 4.5 17.4 1.0
CD2 A:HIS215 4.6 13.5 1.0
CE1 A:PHE59 4.6 16.9 1.0
NE2 A:HIS215 4.7 13.2 1.0
CE2 A:PHE63 4.7 17.7 1.0
CD2 B:DAH98 4.8 18.2 1.0
NE2 A:HIS54 4.8 37.2 1.0
CE1 A:PHE63 4.9 17.3 1.0
CZ A:PHE212 4.9 15.5 1.0
NE2 A:HIS38 4.9 19.2 1.0
CZ A:PHE59 4.9 18.2 1.0
CD2 A:HIS54 5.0 35.6 1.0

Copper binding site 4 out of 5 in 5z0m

Go back to Copper Binding Sites List in 5z0m
Copper binding site 4 out of 5 in the Crystal Structure of Copper-Bound H63F-Mutated Tyrosinase From Streptomyces Castaneoglobisporus in Complex with the Caddie Protein Obtained By Soaking in the Hydroxylamine-Containing Solution For 12 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 H63F-Mutated Tyrosinase From Streptomyces Castaneoglobisporus in Complex with the Caddie Protein Obtained By Soaking in the Hydroxylamine-Containing Solution For 12 H at 298 K within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu201

b:28.4
occ:0.46
 SD B:MET84 1.9 27.8 0.5
NE2 B:HIS82 2.1 22.5 0.5
N B:NO3202 2.2 25.0 0.5
NE2 B:HIS97 2.3 25.5 0.5
O1 B:NO3202 2.4 25.6 0.5
O3 B:NO3202 2.6 22.7 0.5
CE B:MET84 2.7 28.2 0.5
CE1 B:HIS97 2.7 25.7 0.5
O2 B:NO3202 2.8 26.5 0.5
CG B:MET84 2.9 25.9 0.5
SD B:MET84 3.0 29.5 0.5
CE1 B:HIS82 3.0 22.4 0.5
CE1 B:HIS97 3.0 25.8 0.5
CD2 B:HIS82 3.1 22.2 0.5
CE B:MET84 3.1 29.5 0.5
O A:ILE42 3.3 28.2 1.0
CB B:MET84 3.4 24.6 0.5
CB B:MET84 3.4 24.6 0.5
ND1 B:HIS97 3.5 25.6 0.5
ND1 B:HIS82 3.5 22.5 0.5
CD2 B:HIS97 3.6 25.6 0.5
CG B:MET84 3.6 26.2 0.5
CE1 B:HIS82 3.7 22.6 0.5
CA A:MET43 3.8 30.0 1.0
ND1 B:HIS97 4.0 25.4 0.5
ND1 B:HIS82 4.1 22.2 0.5
O A:MET43 4.1 33.5 1.0
NE2 B:HIS97 4.2 25.6 0.5
CG B:HIS82 4.2 21.9 0.5
C A:ILE42 4.3 28.9 1.0
C A:MET43 4.3 30.6 1.0
CG B:HIS97 4.4 25.0 0.5
N A:MET43 4.6 29.6 1.0
O A:HOH445 4.6 36.8 1.0
CA B:MET84 4.7 22.4 1.0
CB A:MET43 4.8 32.6 1.0
N B:MET84 4.8 19.8 1.0
CD1 B:ILE92 4.8 28.0 1.0
CG A:MET43 4.8 35.6 1.0
CG1 B:ILE92 4.9 21.2 1.0
CG B:HIS97 4.9 25.0 0.5
CG B:HIS82 4.9 22.0 0.5
C B:VAL83 5.0 19.0 1.0
NE2 B:HIS82 5.0 22.5 0.5

Copper binding site 5 out of 5 in 5z0m

Go back to Copper Binding Sites List in 5z0m
Copper binding site 5 out of 5 in the Crystal Structure of Copper-Bound H63F-Mutated Tyrosinase From Streptomyces Castaneoglobisporus in Complex with the Caddie Protein Obtained By Soaking in the Hydroxylamine-Containing Solution For 12 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 H63F-Mutated Tyrosinase From Streptomyces Castaneoglobisporus in Complex with the Caddie Protein Obtained By Soaking in the Hydroxylamine-Containing Solution For 12 H at 298 K within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu201

b:41.8
occ:0.54
 NE2 B:HIS82 2.0 22.5 0.5
CD2 B:HIS82 2.9 22.1 0.5
CE1 B:HIS82 3.0 22.6 0.5
ND1 B:HIS82 3.5 22.2 0.5
CE1 B:HIS82 3.7 22.4 0.5
O A:MET43 4.0 33.5 1.0
ND1 B:HIS82 4.0 22.5 0.5
CG B:HIS82 4.1 22.0 0.5
CG B:HIS82 4.8 21.9 0.5
O B:HOH306 4.8 61.6 1.0
NE2 B:HIS82 4.9 22.5 0.5

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: Wed Jul 31 05:29:58 2024

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