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

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 Low

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 Low:
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 Low, PDB code: 3awv 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 / 1.40
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 65.090, 97.850, 55.100, 90.00, 90.00, 90.00
R / Rfree (%) 17.5 / 21.8

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 Low (pdb code 3awv). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 4 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 Low, PDB code: 3awv:
Jump to Copper binding site number: 1; 2; 3; 4;

Copper binding site 1 out of 4 in 3awv

Go back to Copper Binding Sites List in 3awv
Copper binding site 1 out of 4 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 Low


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 Low within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu500

b:17.9
occ:0.62
 O A:HOH545 1.8 16.3 1.0
O A:HOH581 1.9 20.7 1.0
NE2 A:HIS54 2.1 15.2 0.6
NE2 A:HIS38 2.1 21.0 1.0
NE2 A:HIS63 2.7 12.0 1.0
CE1 A:HIS38 2.9 22.9 1.0
CD2 A:HIS54 2.9 15.8 0.6
CE1 A:HIS54 3.2 13.0 0.6
CU A:CU501 3.2 13.5 0.8
CE1 A:HIS63 3.2 10.1 1.0
CD2 A:HIS38 3.3 21.4 1.0
OH B:TYR98 3.8 28.0 1.0
CD2 A:HIS63 3.9 10.4 1.0
NE2 A:HIS216 4.0 14.0 1.0
ND1 A:HIS38 4.1 17.0 1.0
CD1 A:ILE42 4.1 35.8 1.0
CG A:HIS54 4.1 14.5 0.6
ND1 A:HIS54 4.2 13.2 0.6
CE2 A:PHE212 4.3 10.8 1.0
CG A:HIS38 4.3 16.4 1.0
CE1 A:HIS216 4.3 13.6 1.0
CG1 A:ILE42 4.4 28.4 1.0
CZ A:PHE212 4.4 9.6 1.0
ND1 A:HIS63 4.5 10.2 1.0
NE2 A:HIS190 4.6 11.7 1.0
CE2 B:TYR98 4.8 18.5 1.0
NE2 A:HIS194 4.8 11.1 1.0
CZ B:TYR98 4.8 18.7 1.0
CG A:HIS63 4.8 8.3 1.0
CE1 A:PHE59 4.9 9.7 1.0
CD2 A:HIS216 5.0 12.1 1.0
CE1 A:HIS190 5.0 11.0 1.0

Copper binding site 2 out of 4 in 3awv

Go back to Copper Binding Sites List in 3awv
Copper binding site 2 out of 4 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 Low


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 Low within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu501

b:13.5
occ:0.85
 O A:HOH545 1.7 16.3 1.0
NE2 A:HIS190 2.0 11.7 1.0
NE2 A:HIS194 2.1 11.1 1.0
O A:HOH581 2.2 20.7 1.0
NE2 A:HIS216 2.3 14.0 1.0
CE1 A:HIS190 2.9 11.0 1.0
CE1 A:HIS216 3.0 13.6 1.0
CE1 A:HIS194 3.1 9.9 1.0
CD2 A:HIS190 3.1 10.7 1.0
CD2 A:HIS194 3.2 10.2 1.0
CU A:CU500 3.2 17.9 0.6
CD2 A:HIS216 3.4 12.1 1.0
OH B:TYR98 4.0 28.0 1.0
ND1 A:HIS190 4.0 10.0 1.0
CE2 B:TYR98 4.1 18.5 1.0
CG A:HIS190 4.2 10.6 1.0
ND1 A:HIS194 4.2 9.6 1.0
ND1 A:HIS216 4.2 10.8 1.0
CG A:HIS194 4.3 9.2 1.0
CE2 A:PHE212 4.3 10.8 1.0
CZ B:TYR98 4.3 18.7 1.0
CG A:HIS216 4.4 11.7 1.0
NE2 A:HIS63 4.4 12.0 1.0
CE1 A:PHE59 4.6 9.7 1.0
CD2 A:HIS215 4.7 12.6 1.0
NE2 A:HIS215 4.8 14.2 1.0
NE2 A:HIS38 4.8 21.0 1.0
NE2 A:HIS54 4.9 15.2 0.6
CZ A:PHE212 4.9 9.6 1.0
CZ A:PHE59 4.9 10.7 1.0
CD2 B:TYR98 5.0 16.0 1.0
CD2 A:HIS54 5.0 15.8 0.6
CD2 A:HIS63 5.0 10.4 1.0

Copper binding site 3 out of 4 in 3awv

Go back to Copper Binding Sites List in 3awv
Copper binding site 3 out of 4 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 Low


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 Low within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu502

b:21.4
occ:0.72
 OE1 B:GLU67 1.6 36.6 1.0
NE2 B:HIS82 1.9 26.2 1.0
ND1 B:HIS68 2.0 31.4 1.0
O B:HIS68 2.0 41.8 1.0
N B:HIS68 2.5 35.6 1.0
O B:HOH810 2.6 44.5 1.0
C B:HIS68 2.6 43.1 1.0
CD B:GLU67 2.8 38.6 1.0
CA B:HIS68 2.9 37.4 1.0
CE1 B:HIS68 2.9 30.5 1.0
CE1 B:HIS82 2.9 22.0 1.0
CD2 B:HIS82 3.0 24.8 1.0
CG B:HIS68 3.0 33.8 1.0
C B:GLU67 3.3 34.6 1.0
CB B:HIS68 3.4 36.8 1.0
CB B:GLU67 3.4 34.2 1.0
OE2 B:GLU67 3.6 42.4 1.0
CG B:GLU67 3.7 35.6 1.0
N B:GLY69 3.8 48.6 1.0
CA B:GLU67 4.0 34.5 1.0
ND1 B:HIS82 4.0 22.2 1.0
NE2 B:HIS68 4.0 28.9 1.0
CG B:HIS82 4.1 22.1 1.0
CD2 B:HIS68 4.1 30.2 1.0
O B:GLU67 4.1 32.8 1.0
O A:MET43 4.2 22.5 1.0
N B:GLY70 4.3 54.1 1.0
CA B:GLY69 4.7 53.8 1.0
C B:GLY69 4.7 57.6 1.0
O B:HOH622 4.7 23.2 1.0
CA B:GLY70 4.9 50.5 1.0

Copper binding site 4 out of 4 in 3awv

Go back to Copper Binding Sites List in 3awv
Copper binding site 4 out of 4 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 Low


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 Low within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu502

b:24.6
occ:0.20
 CE B:MET84 2.2 37.9 0.7
SD B:MET84 2.3 41.8 0.3
N B:NO3508 2.4 25.0 0.7
CG B:MET84 2.4 19.1 0.3
O1 B:NO3508 2.5 31.1 0.7
O3 B:NO3508 2.6 23.9 0.7
O2 B:NO3508 2.9 18.6 0.7
SD B:MET84 3.1 33.4 0.7
CB B:MET84 3.2 17.9 0.7
CB B:MET84 3.3 17.9 0.3
CE1 B:HIS97 3.5 23.0 1.0
O A:ILE42 3.5 19.2 1.0
CE1 B:HIS82 3.7 22.0 1.0
ND1 B:HIS82 3.7 22.2 1.0
CG B:MET84 3.8 22.6 0.7
CE B:MET84 3.9 30.1 0.3
ND1 B:HIS97 3.9 20.0 1.0
O A:HOH717 3.9 30.6 1.0
CA A:MET43 4.0 17.9 1.0
O A:MET43 4.0 22.5 1.0
C A:MET43 4.3 18.6 1.0
C A:ILE42 4.5 15.4 1.0
CA B:MET84 4.6 12.8 1.0
N B:MET84 4.7 13.9 1.0
N A:MET43 4.7 14.9 1.0
NE2 B:HIS97 4.7 25.1 1.0
CD1 B:ILE92 4.8 19.7 1.0
C B:VAL83 4.8 14.0 1.0
CG1 B:ILE92 4.9 13.0 1.0
O B:VAL83 4.9 15.7 1.0
CB A:MET43 4.9 18.6 1.0
NE2 B:HIS82 5.0 26.2 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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