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Copper in PDB 5z0g: Crystal Structure of Copper-Bound Tyrosinase From Streptomyces Castaneoglobisporus in Complex with the Caddie Protein Obtained By Soaking in the Hydroxylamine-Containing Solution For 20 Min 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 20 Min 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 20 Min 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 20 Min at 298 K, PDB code: 5z0g 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 / 1.32
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 65.200, 97.790, 55.100, 90.00, 90.00, 90.00
R / Rfree (%) 14 / 18.7

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 20 Min at 298 K (pdb code 5z0g). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 8 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 20 Min at 298 K, PDB code: 5z0g:
Jump to Copper binding site number: 1; 2; 3; 4; 5; 6; 7; 8;

Copper binding site 1 out of 8 in 5z0g

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Copper binding site 1 out of 8 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 20 Min 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 20 Min at 298 K within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu301

b:14.9
occ:0.55
 CU A:CU301 0.0 14.9 0.6
CU A:CU301 1.2 13.8 0.2
NE2 A:HIS38 1.8 13.8 0.7
NE2 A:HIS63 1.9 12.1 1.0
NE2 A:HIS54 2.2 16.3 0.7
CE1 A:HIS54 2.3 15.5 0.3
NE2 A:HIS54 2.3 15.6 0.3
NE2 A:HIS38 2.4 14.3 0.3
O A:HOH501 2.6 13.7 0.7
CD2 A:HIS38 2.6 14.0 0.3
CE1 A:HIS63 2.7 12.2 1.0
O2 A:PER304 2.7 14.1 0.3
CD2 A:HIS38 2.7 14.8 0.7
CU A:CU301 2.8 14.0 0.3
CE1 A:HIS38 2.9 13.9 0.7
O1 A:PER304 2.9 13.4 0.3
CD2 A:HIS63 3.1 11.1 1.0
CE1 A:HIS54 3.2 15.3 0.7
CD2 A:HIS54 3.2 15.6 0.7
ND1 A:HIS54 3.4 15.0 0.3
CD2 A:HIS54 3.5 15.1 0.3
CE1 A:HIS38 3.7 14.1 0.3
CG A:HIS38 3.9 14.0 0.7
ND1 A:HIS38 3.9 13.5 0.7
ND1 A:HIS63 3.9 10.7 1.0
CG A:HIS38 3.9 13.7 0.3
CZ A:PHE212 4.0 9.9 1.0
CG A:HIS54 4.1 14.4 0.3
CG A:HIS63 4.1 10.2 1.0
CU A:CU302 4.2 11.9 0.5
ND1 A:HIS54 4.3 14.2 0.7
CZ3 A:TRP62 4.3 11.9 1.0
CG A:HIS54 4.3 13.8 0.7
CE2 A:PHE212 4.3 10.8 1.0
NE2 A:HIS216 4.4 10.5 1.0
ND1 A:HIS38 4.4 13.6 0.3
OE2 B:DAH98 4.5 14.3 0.2
CE1 A:HIS216 4.5 11.9 1.0
CU A:CU302 4.6 11.3 0.6
OZ B:DAH98 4.8 16.1 1.0
CE3 A:TRP62 4.9 10.5 1.0
O A:GLY53 4.9 12.1 1.0
CD1 A:ILE42 5.0 29.4 1.0

Copper binding site 2 out of 8 in 5z0g

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Copper binding site 2 out of 8 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 20 Min 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 20 Min at 298 K within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu301

b:13.8
occ:0.16
 CU A:CU301 0.0 13.8 0.2
CU A:CU301 1.2 14.9 0.6
O A:HOH501 1.6 13.7 0.7
O2 A:PER304 1.7 14.1 0.3
NE2 A:HIS54 1.7 15.6 0.3
CU A:CU301 1.9 14.0 0.3
O1 A:PER304 2.1 13.4 0.3
NE2 A:HIS38 2.2 13.8 0.7
NE2 A:HIS54 2.2 16.3 0.7
NE2 A:HIS38 2.3 14.3 0.3
CE1 A:HIS54 2.3 15.5 0.3
NE2 A:HIS63 2.6 12.1 1.0
CE1 A:HIS38 2.7 13.9 0.7
CD2 A:HIS54 2.9 15.6 0.7
CD2 A:HIS54 2.9 15.1 0.3
CD2 A:HIS38 3.1 14.0 0.3
OE2 B:DAH98 3.3 14.3 0.2
CE1 A:HIS63 3.3 12.2 1.0
CU A:CU302 3.4 11.9 0.5
CE1 A:HIS54 3.4 15.3 0.7
CE1 A:HIS38 3.4 14.1 0.3
CD2 A:HIS38 3.4 14.8 0.7
ND1 A:HIS54 3.5 15.0 0.3
OZ B:DAH98 3.8 16.1 1.0
CG A:HIS54 3.8 14.4 0.3
CD2 A:HIS63 3.8 11.1 1.0
CU A:CU302 3.9 11.3 0.6
ND1 A:HIS38 4.0 13.5 0.7
NE2 A:HIS216 4.1 10.5 1.0
CG A:HIS54 4.1 13.8 0.7
CE2 A:PHE212 4.3 10.8 1.0
ND1 A:HIS54 4.3 14.2 0.7
CZ A:PHE212 4.3 9.9 1.0
CG A:HIS38 4.3 13.7 0.3
CG A:HIS38 4.3 14.0 0.7
CD1 A:ILE42 4.4 29.4 1.0
CE1 A:HIS216 4.4 11.9 1.0
ND1 A:HIS38 4.4 13.6 0.3
ND1 A:HIS63 4.5 10.7 1.0
CE2 B:DAH98 4.6 15.3 1.0
CZ B:DAH98 4.7 14.7 1.0
NE2 A:HIS190 4.7 11.1 1.0
CG1 A:ILE42 4.7 21.6 1.0
CG A:HIS63 4.8 10.2 1.0
CE1 A:PHE59 4.8 10.2 1.0
CE1 A:HIS190 5.0 10.6 1.0

Copper binding site 3 out of 8 in 5z0g

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Copper binding site 3 out of 8 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 20 Min 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 20 Min at 298 K within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu301

b:14.0
occ:0.29
 CU A:CU301 0.0 14.0 0.3
CU A:CU301 1.9 13.8 0.2
O A:HOH501 1.9 13.7 0.7
O2 A:PER304 2.0 14.1 0.3
OZ B:DAH98 2.1 16.1 1.0
O1 A:PER304 2.1 13.4 0.3
NE2 A:HIS54 2.2 15.6 0.3
NE2 A:HIS38 2.2 14.3 0.3
OE2 B:DAH98 2.2 14.3 0.2
CE1 A:HIS38 2.4 13.9 0.7
CE1 A:HIS38 2.6 14.1 0.3
NE2 A:HIS38 2.8 13.8 0.7
CU A:CU301 2.8 14.9 0.6
NE2 A:HIS54 2.9 16.3 0.7
CD1 A:ILE42 3.1 29.4 1.0
CZ B:DAH98 3.1 14.7 1.0
CE1 A:HIS54 3.1 15.5 0.3
CD2 A:HIS54 3.1 15.1 0.3
CE2 B:DAH98 3.3 15.3 1.0
CD2 A:HIS54 3.4 15.6 0.7
CD2 A:HIS38 3.5 14.0 0.3
CG1 A:ILE42 3.6 21.6 1.0
ND1 A:HIS38 3.6 13.5 0.7
CU A:CU302 3.7 11.9 0.5
CE1 A:HIS54 3.9 15.3 0.7
ND1 A:HIS38 3.9 13.6 0.3
OG A:SER206 4.1 12.0 1.0
CD2 A:HIS38 4.1 14.8 0.7
ND1 A:HIS54 4.2 15.0 0.3
CG A:HIS54 4.2 14.4 0.3
O B:HOH314 4.2 29.2 1.0
CU A:CU302 4.3 11.3 0.6
CE1 B:DAH98 4.4 13.4 1.0
CG A:HIS38 4.4 13.7 0.3
CG A:HIS54 4.5 13.8 0.7
NE2 A:HIS63 4.5 12.1 1.0
CG A:HIS38 4.5 14.0 0.7
CD2 B:DAH98 4.6 14.2 1.0
NE2 A:HIS194 4.6 10.8 1.0
CE2 A:PHE212 4.7 10.8 1.0
CE1 A:HIS194 4.7 11.9 1.0
ND1 A:HIS54 4.7 14.2 0.7

Copper binding site 4 out of 8 in 5z0g

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Copper binding site 4 out of 8 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 20 Min 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 20 Min at 298 K within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu302

b:11.3
occ:0.55
 CU A:CU302 0.0 11.3 0.6
CU A:CU302 0.8 11.9 0.5
NE2 A:HIS216 1.9 10.5 1.0
NE2 A:HIS194 1.9 10.8 1.0
NE2 A:HIS190 2.2 11.1 1.0
O1 A:PER304 2.3 13.4 0.3
O A:HOH501 2.5 13.7 0.7
O2 A:PER304 2.7 14.1 0.3
CE1 A:HIS194 2.8 11.9 1.0
CD2 A:HIS216 2.9 10.3 1.0
CE1 A:HIS216 2.9 11.9 1.0
CD2 A:HIS194 3.0 10.0 1.0
CD2 A:HIS190 3.0 10.0 1.0
CE1 A:HIS190 3.3 10.6 1.0
OE2 B:DAH98 3.8 14.3 0.2
CE2 A:PHE212 3.9 10.8 1.0
CD2 A:HIS215 3.9 11.3 1.0
CU A:CU301 3.9 13.8 0.2
ND1 A:HIS216 4.0 11.2 1.0
CG A:HIS216 4.0 10.1 1.0
ND1 A:HIS194 4.0 11.9 1.0
CG A:HIS194 4.1 9.9 1.0
NE2 A:HIS215 4.1 12.1 1.0
CG A:HIS190 4.2 9.8 1.0
CU A:CU301 4.3 14.0 0.3
ND1 A:HIS190 4.3 10.9 1.0
OZ B:DAH98 4.3 16.1 1.0
CE2 B:DAH98 4.4 15.3 1.0
CD2 A:PHE212 4.5 9.8 1.0
CZ A:PHE212 4.5 9.9 1.0
CZ B:DAH98 4.6 14.7 1.0
CU A:CU301 4.6 14.9 0.6
NE2 A:HIS63 4.9 12.1 1.0

Copper binding site 5 out of 8 in 5z0g

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Copper binding site 5 out of 8 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 20 Min 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 20 Min at 298 K within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu302

b:11.9
occ:0.45
 CU A:CU302 0.0 11.9 0.5
CU A:CU302 0.8 11.3 0.6
O1 A:PER304 1.9 13.4 0.3
O A:HOH501 1.9 13.7 0.7
NE2 A:HIS190 2.0 11.1 1.0
O2 A:PER304 2.0 14.1 0.3
NE2 A:HIS194 2.2 10.8 1.0
NE2 A:HIS216 2.2 10.5 1.0
CE1 A:HIS190 2.8 10.6 1.0
CE1 A:HIS216 3.0 11.9 1.0
CD2 A:HIS190 3.1 10.0 1.0
OE2 B:DAH98 3.1 14.3 0.2
CE1 A:HIS194 3.1 11.9 1.0
CD2 A:HIS194 3.2 10.0 1.0
CU A:CU301 3.4 13.8 0.2
CD2 A:HIS216 3.4 10.3 1.0
CU A:CU301 3.7 14.0 0.3
CE2 B:DAH98 3.9 15.3 1.0
OZ B:DAH98 3.9 16.1 1.0
ND1 A:HIS190 4.0 10.9 1.0
CE2 A:PHE212 4.1 10.8 1.0
CG A:HIS190 4.1 9.8 1.0
CU A:CU301 4.2 14.9 0.6
ND1 A:HIS216 4.2 11.2 1.0
ND1 A:HIS194 4.2 11.9 1.0
CZ B:DAH98 4.2 14.7 1.0
CG A:HIS194 4.3 9.9 1.0
CG A:HIS216 4.4 10.1 1.0
NE2 A:HIS54 4.4 15.6 0.3
NE2 A:HIS63 4.5 12.1 1.0
CD2 A:HIS215 4.6 11.3 1.0
NE2 A:HIS215 4.7 12.1 1.0
CZ A:PHE212 4.7 9.9 1.0
CE1 A:PHE59 4.7 10.2 1.0
CD2 B:DAH98 4.7 14.2 1.0
CD2 A:PHE212 4.9 9.8 1.0
NE2 A:HIS38 4.9 13.8 0.7
CD2 A:HIS54 4.9 15.1 0.3
NE2 A:HIS38 4.9 14.3 0.3

Copper binding site 6 out of 8 in 5z0g

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Copper binding site 6 out of 8 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 20 Min 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 20 Min at 298 K within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu303

b:40.8
occ:0.50
 NE2 A:HIS277 1.9 50.0 1.0
O A:HOH717 2.4 27.1 0.5
CE1 A:HIS277 2.6 50.4 1.0
CD2 A:HIS277 3.1 50.6 1.0
ND1 A:HIS277 3.9 51.4 1.0
CG A:HIS277 4.1 51.9 1.0
CG A:PRO231 4.5 23.1 1.0
O A:HOH587 4.8 35.2 1.0

Copper binding site 7 out of 8 in 5z0g

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Copper binding site 7 out of 8 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 20 Min at 298 K


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 7 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 20 Min at 298 K within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu201

b:29.9
occ:0.45
 NE2 B:HIS82 2.5 19.2 0.5
CD2 B:HIS82 3.1 19.1 0.5
CE1 B:HIS82 3.5 18.6 0.5
ND1 B:HIS82 3.6 18.2 0.6
CE1 B:HIS82 3.6 18.2 0.6
O A:MET43 4.0 23.5 1.0
CG B:HIS82 4.3 17.5 0.5
ND1 B:HIS82 4.5 17.9 0.5
O B:HOH352 4.7 25.0 1.0
CG B:HIS82 4.9 17.2 0.6
NE2 B:HIS82 5.0 17.9 0.6

Copper binding site 8 out of 8 in 5z0g

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Copper binding site 8 out of 8 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 20 Min at 298 K


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 8 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 20 Min at 298 K within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu201

b:17.8
occ:0.55
 NE2 B:HIS82 1.9 17.9 0.6
O1 B:NO3202 1.9 22.2 0.5
CE B:MET84 2.1 19.1 0.5
NE2 B:HIS97 2.1 18.6 0.6
N B:NO3202 2.2 17.8 0.5
SD B:MET84 2.2 18.1 0.6
O3 B:NO3202 2.4 17.1 0.5
CE1 B:HIS82 2.8 18.2 0.6
CE1 B:HIS82 2.9 18.6 0.5
CE1 B:HIS97 2.9 17.5 0.6
CD2 B:HIS82 3.0 17.4 0.6
O2 B:NO3202 3.0 17.6 0.5
CG B:MET84 3.2 19.0 0.6
ND1 B:HIS82 3.2 17.9 0.5
CD2 B:HIS97 3.2 18.5 0.6
CE B:MET84 3.3 18.7 0.6
O A:ILE42 3.3 16.4 1.0
SD B:MET84 3.4 21.2 0.5
CB B:MET84 3.5 18.4 1.0
CA A:MET43 3.7 16.7 1.0
CE1 B:HIS97 3.9 17.4 0.5
ND1 B:HIS82 3.9 18.2 0.6
O A:MET43 4.0 23.5 1.0
CG B:MET84 4.0 19.0 0.5
CG B:HIS82 4.1 17.2 0.6
ND1 B:HIS97 4.1 16.9 0.5
ND1 B:HIS97 4.1 16.6 0.6
C A:ILE42 4.1 17.1 1.0
NE2 B:HIS82 4.2 19.2 0.5
C A:MET43 4.2 16.6 1.0
CG B:HIS97 4.3 17.4 0.6
N A:MET43 4.4 16.1 1.0
CG B:HIS82 4.5 17.5 0.5
CG2 A:ILE42 4.6 25.7 1.0
CB A:MET43 4.6 17.8 1.0
CG A:MET43 4.6 18.0 1.0
CA B:MET84 4.8 13.8 1.0
N B:MET84 4.8 13.3 1.0
O A:HOH575 4.8 18.8 1.0
C B:VAL83 4.9 13.1 1.0
O B:VAL83 4.9 15.6 1.0
CD2 B:HIS82 5.0 19.1 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 05:28:28 2024

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