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Copper in PDB 3awz: Crystal Structure of Streptomyces Tyrosinase in A Complex with Caddie H97Q Mutant Soaked in A Cu(II)-Containing Solution For 80 Hr

Enzymatic activity of Crystal Structure of Streptomyces Tyrosinase in A Complex with Caddie H97Q Mutant Soaked in A Cu(II)-Containing Solution For 80 Hr

All present enzymatic activity of Crystal Structure of Streptomyces Tyrosinase in A Complex with Caddie H97Q Mutant Soaked in A Cu(II)-Containing Solution For 80 Hr:
1.14.18.1;

Protein crystallography data

The structure of Crystal Structure of Streptomyces Tyrosinase in A Complex with Caddie H97Q Mutant Soaked in A Cu(II)-Containing Solution For 80 Hr, PDB code: 3awz 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 / 1.43
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 64.420, 96.380, 54.490, 90.00, 90.00, 90.00
R / Rfree (%) 17.9 / 22.2

Copper Binding Sites:

The binding sites of Copper atom in the Crystal Structure of Streptomyces Tyrosinase in A Complex with Caddie H97Q Mutant Soaked in A Cu(II)-Containing Solution For 80 Hr (pdb code 3awz). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 3 binding sites of Copper where determined in the Crystal Structure of Streptomyces Tyrosinase in A Complex with Caddie H97Q Mutant Soaked in A Cu(II)-Containing Solution For 80 Hr, PDB code: 3awz:
Jump to Copper binding site number: 1; 2; 3;

Copper binding site 1 out of 3 in 3awz

Go back to Copper Binding Sites List in 3awz
Copper binding site 1 out of 3 in the Crystal Structure of Streptomyces Tyrosinase in A Complex with Caddie H97Q Mutant Soaked in A Cu(II)-Containing Solution For 80 Hr


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 H97Q Mutant Soaked in A Cu(II)-Containing Solution For 80 Hr within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu500

b:21.8
occ:0.35
NE2 A:HIS190 2.0 13.4 1.0
NE2 A:HIS194 2.0 13.5 1.0
NE2 A:HIS216 2.0 17.0 1.0
O B:HOH533 2.2 16.6 1.0
CE1 A:HIS216 2.4 13.6 1.0
CD2 A:HIS190 2.8 13.6 1.0
CD2 A:HIS194 2.9 12.6 1.0
CE1 A:HIS194 3.0 12.8 1.0
CE1 A:HIS190 3.1 12.5 1.0
CD2 A:HIS216 3.4 15.1 1.0
ND1 A:HIS216 3.8 15.2 1.0
OH B:TYR98 3.8 14.7 1.0
CE2 B:TYR98 3.8 11.9 1.0
CG A:HIS190 4.0 12.8 1.0
CG A:HIS194 4.0 11.9 1.0
ND1 A:HIS194 4.1 12.3 1.0
ND1 A:HIS190 4.1 13.1 1.0
CG A:HIS216 4.2 13.3 1.0
CZ B:TYR98 4.2 12.9 1.0
CE2 A:PHE212 4.2 10.8 1.0
CD2 A:HIS215 4.5 14.5 1.0
NE2 A:HIS215 4.6 14.6 1.0
NE2 A:HIS63 4.8 12.2 1.0
CD2 B:TYR98 4.8 10.6 1.0
CZ A:PHE212 4.8 11.8 1.0
CD2 A:PHE212 4.9 10.2 1.0
CE1 A:PHE59 4.9 10.3 1.0
NE2 A:HIS54 5.0 16.1 1.0

Copper binding site 2 out of 3 in 3awz

Go back to Copper Binding Sites List in 3awz
Copper binding site 2 out of 3 in the Crystal Structure of Streptomyces Tyrosinase in A Complex with Caddie H97Q Mutant Soaked in A Cu(II)-Containing Solution For 80 Hr


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 H97Q Mutant Soaked in A Cu(II)-Containing Solution For 80 Hr within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu502

b:32.9
occ:0.50
NE2 A:HIS277 1.9 30.9 1.0
NE2 A:HIS279 2.2 41.1 1.0
O A:HOH728 2.6 31.5 0.5
CE1 A:HIS277 2.8 31.7 1.0
CD2 A:HIS277 3.0 31.0 1.0
CE1 A:HIS279 3.1 41.3 1.0
CD2 A:HIS279 3.3 38.6 1.0
ND1 A:HIS277 3.9 33.7 1.0
CG A:HIS277 4.0 35.7 1.0
ND1 A:HIS279 4.3 39.2 1.0
CG A:HIS279 4.4 39.3 1.0
CG A:PRO231 4.7 26.8 1.0

Copper binding site 3 out of 3 in 3awz

Go back to Copper Binding Sites List in 3awz
Copper binding site 3 out of 3 in the Crystal Structure of Streptomyces Tyrosinase in A Complex with Caddie H97Q Mutant Soaked in A Cu(II)-Containing Solution For 80 Hr


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 H97Q Mutant Soaked in A Cu(II)-Containing Solution For 80 Hr within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu501

b:27.1
occ:0.75
OE1 B:GLU67 1.6 40.8 1.0
O B:HIS68 2.0 46.9 1.0
ND1 B:HIS68 2.0 38.7 1.0
NE2 B:HIS82 2.1 25.3 1.0
N B:HIS68 2.7 36.2 1.0
CE1 B:HIS68 2.8 38.0 1.0
C B:HIS68 2.8 44.9 1.0
CD B:GLU67 2.9 42.8 1.0
CD2 B:HIS82 2.9 24.4 1.0
CE1 B:HIS82 3.1 23.2 1.0
CA B:HIS68 3.2 36.9 1.0
CG B:HIS68 3.2 36.1 1.0
CB B:GLU67 3.2 35.6 1.0
C B:GLU67 3.2 37.3 1.0
CG B:GLU67 3.7 39.1 1.0
CB B:HIS68 3.7 33.4 1.0
OE2 B:GLU67 3.8 46.6 1.0
CA B:GLU67 3.8 36.0 1.0
O B:GLU67 3.9 41.2 1.0
NE2 B:HIS68 4.0 37.2 1.0
N B:GLY69 4.0 50.9 1.0
N B:GLY70 4.0 57.5 1.0
O A:MET43 4.1 18.8 1.0
CG B:HIS82 4.1 21.2 1.0
ND1 B:HIS82 4.2 21.5 1.0
CD2 B:HIS68 4.2 38.2 1.0
CA B:GLY70 4.5 53.0 1.0
CA B:GLY69 4.5 55.1 1.0
C B:GLY69 4.6 57.4 1.0
O B:HOH643 4.8 26.1 1.0
N B:GLU67 5.0 34.7 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: Wed Jul 31 00:42:19 2024

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