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Copper in PDB 3aww: Crystal Structure of Streptomyces Tyrosinase in A Complex with Caddie Soaked in A Cu(II)-Containing Solution For 80 Hr: Occupancy of Cua Is High

Enzymatic activity of Crystal Structure of Streptomyces Tyrosinase in A Complex with Caddie Soaked in A Cu(II)-Containing Solution For 80 Hr: Occupancy of Cua Is High

All present enzymatic activity of Crystal Structure of Streptomyces Tyrosinase in A Complex with Caddie Soaked in A Cu(II)-Containing Solution For 80 Hr: Occupancy of Cua Is High:
1.14.18.1;

Protein crystallography data

The structure of Crystal Structure of Streptomyces Tyrosinase in A Complex with Caddie Soaked in A Cu(II)-Containing Solution For 80 Hr: Occupancy of Cua Is High, PDB code: 3aww 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 / 1.35
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 65.360, 98.230, 55.170, 90.00, 90.00, 90.00
R / Rfree (%) 18 / 21.6

Copper Binding Sites:

The binding sites of Copper atom in the Crystal Structure of Streptomyces Tyrosinase in A Complex with Caddie Soaked in A Cu(II)-Containing Solution For 80 Hr: Occupancy of Cua Is High (pdb code 3aww). 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 Streptomyces Tyrosinase in A Complex with Caddie Soaked in A Cu(II)-Containing Solution For 80 Hr: Occupancy of Cua Is High, PDB code: 3aww:
Jump to Copper binding site number: 1; 2; 3; 4; 5;

Copper binding site 1 out of 5 in 3aww

Go back to Copper Binding Sites List in 3aww
Copper binding site 1 out of 5 in the Crystal Structure of Streptomyces Tyrosinase in A Complex with Caddie Soaked in A Cu(II)-Containing Solution For 80 Hr: Occupancy of Cua Is High


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 Streptomyces Tyrosinase in A Complex with Caddie Soaked in A Cu(II)-Containing Solution For 80 Hr: Occupancy of Cua Is High within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu500

b:16.9
occ:0.72
 CU A:CU500 0.0 16.9 0.7
CU A:CU500 1.4 21.9 0.2
O A:HOH567 1.9 17.4 1.0
O B:HOH541 2.0 14.8 1.0
NE2 A:HIS54 2.1 19.0 1.0
NE2 A:HIS38 2.1 17.1 1.0
NE2 A:HIS63 2.6 12.0 1.0
CD2 A:HIS54 2.8 19.1 1.0
CE1 A:HIS38 2.8 19.0 1.0
CE1 A:HIS63 3.2 9.5 1.0
CD2 A:HIS38 3.2 15.7 1.0
CE1 A:HIS54 3.2 17.4 1.0
CU A:CU501 3.3 12.6 0.8
OH B:TYR98 3.7 18.3 1.0
CD2 A:HIS63 3.8 11.1 1.0
CG A:HIS54 4.1 17.0 1.0
ND1 A:HIS38 4.1 13.0 1.0
NE2 A:HIS216 4.1 11.0 1.0
ND1 A:HIS54 4.2 14.3 1.0
CG A:HIS38 4.2 11.4 1.0
CD1 A:ILE42 4.3 20.4 1.0
CE2 A:PHE212 4.4 11.4 1.0
ND1 A:HIS63 4.5 9.0 1.0
CZ A:PHE212 4.5 10.5 1.0
CE2 B:TYR98 4.5 14.6 1.0
CE1 A:HIS216 4.5 9.9 1.0
CZ B:TYR98 4.6 14.4 1.0
NE2 A:HIS190 4.7 10.1 1.0
CG A:HIS63 4.8 8.7 1.0
CG1 A:ILE42 4.8 20.0 1.0
NE2 A:HIS194 4.9 9.6 1.0
CE1 A:PHE59 5.0 10.0 1.0

Copper binding site 2 out of 5 in 3aww

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Copper binding site 2 out of 5 in the Crystal Structure of Streptomyces Tyrosinase in A Complex with Caddie Soaked in A Cu(II)-Containing Solution For 80 Hr: Occupancy of Cua Is High


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 Streptomyces Tyrosinase in A Complex with Caddie Soaked in A Cu(II)-Containing Solution For 80 Hr: Occupancy of Cua Is High within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu500

b:21.9
occ:0.21
 CU A:CU500 0.0 21.9 0.2
CU A:CU500 1.4 16.9 0.7
NE2 A:HIS63 1.8 12.0 1.0
NE2 A:HIS38 1.9 17.1 1.0
NE2 A:HIS54 2.1 19.0 1.0
CD2 A:HIS38 2.4 15.7 1.0
CE1 A:HIS63 2.5 9.5 1.0
CE1 A:HIS54 2.8 17.4 1.0
CD2 A:HIS63 3.1 11.1 1.0
O A:HOH567 3.1 17.4 1.0
CE1 A:HIS38 3.1 19.0 1.0
O B:HOH541 3.2 14.8 1.0
CD2 A:HIS54 3.2 19.1 1.0
CG A:HIS38 3.7 11.4 1.0
ND1 A:HIS63 3.7 9.0 1.0
ND1 A:HIS38 4.0 13.0 1.0
ND1 A:HIS54 4.0 14.3 1.0
CG A:HIS63 4.0 8.7 1.0
CZ3 A:TRP62 4.1 10.9 1.0
CG A:HIS54 4.2 17.0 1.0
CZ A:PHE212 4.3 10.5 1.0
CU A:CU501 4.5 12.6 0.8
CE3 A:TRP62 4.6 12.0 1.0
O A:GLY53 4.6 11.6 1.0
NE2 A:HIS216 4.6 11.0 1.0
CE2 A:PHE212 4.6 11.4 1.0
CE1 A:HIS216 4.8 9.9 1.0
CH2 A:TRP62 4.9 12.3 1.0
OH B:TYR98 5.0 18.3 1.0

Copper binding site 3 out of 5 in 3aww

Go back to Copper Binding Sites List in 3aww
Copper binding site 3 out of 5 in the Crystal Structure of Streptomyces Tyrosinase in A Complex with Caddie Soaked in A Cu(II)-Containing Solution For 80 Hr: Occupancy of Cua Is High


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 Streptomyces Tyrosinase in A Complex with Caddie Soaked in A Cu(II)-Containing Solution For 80 Hr: Occupancy of Cua Is High within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu501

b:12.6
occ:0.84
 O B:HOH541 1.8 14.8 1.0
NE2 A:HIS190 2.0 10.1 1.0
NE2 A:HIS194 2.0 9.6 1.0
NE2 A:HIS216 2.2 11.0 1.0
O A:HOH567 2.4 17.4 1.0
CE1 A:HIS190 2.9 10.9 1.0
CE1 A:HIS194 3.0 10.2 1.0
CE1 A:HIS216 3.0 9.9 1.0
CD2 A:HIS190 3.0 9.3 1.0
CD2 A:HIS194 3.1 9.7 1.0
CD2 A:HIS216 3.3 9.8 1.0
CU A:CU500 3.3 16.9 0.7
CE2 B:TYR98 3.8 14.6 1.0
OH B:TYR98 3.9 18.3 1.0
ND1 A:HIS190 4.1 9.6 1.0
CZ B:TYR98 4.1 14.4 1.0
ND1 A:HIS194 4.1 10.4 1.0
CG A:HIS190 4.1 10.0 1.0
CG A:HIS194 4.2 9.5 1.0
ND1 A:HIS216 4.2 9.9 1.0
CE2 A:PHE212 4.3 11.4 1.0
CG A:HIS216 4.4 9.2 1.0
NE2 A:HIS63 4.4 12.0 1.0
CU A:CU500 4.5 21.9 0.2
CD2 A:HIS215 4.6 11.8 1.0
CD2 B:TYR98 4.7 12.6 1.0
CE1 A:PHE59 4.8 10.0 1.0
NE2 A:HIS38 4.8 17.1 1.0
NE2 A:HIS215 4.8 11.3 1.0
CZ A:PHE212 4.9 10.5 1.0
CD2 A:HIS63 4.9 11.1 1.0

Copper binding site 4 out of 5 in 3aww

Go back to Copper Binding Sites List in 3aww
Copper binding site 4 out of 5 in the Crystal Structure of Streptomyces Tyrosinase in A Complex with Caddie Soaked in A Cu(II)-Containing Solution For 80 Hr: Occupancy of Cua Is High


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 Streptomyces Tyrosinase in A Complex with Caddie Soaked in A Cu(II)-Containing Solution For 80 Hr: Occupancy of Cua Is High within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu503

b:39.1
occ:0.50
 NE2 A:HIS277 2.1 43.9 1.0
NE2 A:HIS279 2.4 73.2 1.0
O A:HOH880 2.7 45.0 0.5
CD2 A:HIS279 3.0 74.2 1.0
CD2 A:HIS277 3.1 46.4 1.0
CE1 A:HIS277 3.2 43.5 1.0
CE1 A:HIS279 3.6 74.4 1.0
ND1 A:HIS277 4.2 43.1 1.0
CG A:HIS277 4.2 47.2 1.0
CG A:HIS279 4.3 75.9 1.0
ND1 A:HIS279 4.5 76.0 1.0
CG A:PRO231 4.6 22.9 1.0
O A:HOH810 4.7 32.8 1.0

Copper binding site 5 out of 5 in 3aww

Go back to Copper Binding Sites List in 3aww
Copper binding site 5 out of 5 in the Crystal Structure of Streptomyces Tyrosinase in A Complex with Caddie Soaked in A Cu(II)-Containing Solution For 80 Hr: Occupancy of Cua Is High


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 Streptomyces Tyrosinase in A Complex with Caddie Soaked in A Cu(II)-Containing Solution For 80 Hr: Occupancy of Cua Is High within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu502

b:27.2
occ:0.56
 ND1 B:HIS68 1.9 53.4 1.0
NE2 B:HIS82 2.0 20.7 0.6
O B:HIS68 2.2 55.9 1.0
N B:HIS68 2.4 55.2 1.0
OE1 B:GLU67 2.6 64.2 1.0
CE1 B:HIS68 2.8 52.4 1.0
C B:HIS68 2.8 58.3 1.0
CG B:HIS68 2.9 52.7 1.0
CA B:HIS68 2.9 54.7 1.0
CD2 B:HIS82 3.0 20.1 0.6
CE1 B:HIS82 3.0 17.3 0.6
CB B:GLU67 3.1 59.7 1.0
C B:GLU67 3.3 57.2 1.0
CB B:HIS68 3.3 52.2 1.0
CD B:GLU67 3.7 61.2 1.0
CA B:GLU67 3.8 59.8 1.0
NE2 B:HIS68 3.8 52.9 1.0
CD2 B:HIS68 3.9 52.1 1.0
N B:GLY69 4.0 63.0 1.0
CG B:GLU67 4.0 60.0 1.0
ND1 B:HIS82 4.1 16.2 0.6
O B:GLU67 4.2 57.0 1.0
CG B:HIS82 4.2 17.2 0.6
O A:MET43 4.2 19.1 1.0
ND1 B:HIS82 4.5 15.1 0.4
C B:GLY69 4.6 67.3 1.0
O B:GLY69 4.6 71.2 1.0
OE2 B:GLU67 4.8 59.2 1.0
CA B:GLY69 4.9 65.4 1.0
N B:GLY70 4.9 65.8 1.0
O B:HOH652 4.9 23.4 1.0

Reference:

Y.Matoba, N.Bando, K.Oda, M.Noda, F.Higashikawa, T.Kumagai, M.Sugiyama. A Molecular Mechanism For Copper Transportation to Tyrosinase That Is Assisted By A Metallochaperone, Caddie Protein J.Biol.Chem. V. 286 30219 2011.
ISSN: ISSN 0021-9258
PubMed: 21730070
DOI: 10.1074/JBC.M111.256818
Page generated: Mon Jul 14 01:55:53 2025

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