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Copper in PDB 3awy: Crystal Structure of Streptomyces Tyrosinase in A Complex with Caddie M84L Mutant Soaked in A Cu(II)-Containing Solution For 80 Hr

Enzymatic activity of Crystal Structure of Streptomyces Tyrosinase in A Complex with Caddie M84L 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 M84L 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 M84L Mutant Soaked in A Cu(II)-Containing Solution For 80 Hr, PDB code: 3awy 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 / 1.58
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 64.690, 96.340, 54.650, 90.00, 90.00, 90.00
R / Rfree (%) 19 / 24.2

Copper Binding Sites:

The binding sites of Copper atom in the Crystal Structure of Streptomyces Tyrosinase in A Complex with Caddie M84L Mutant Soaked in A Cu(II)-Containing Solution For 80 Hr (pdb code 3awy). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 6 binding sites of Copper where determined in the Crystal Structure of Streptomyces Tyrosinase in A Complex with Caddie M84L Mutant Soaked in A Cu(II)-Containing Solution For 80 Hr, PDB code: 3awy:
Jump to Copper binding site number: 1; 2; 3; 4; 5; 6;

Copper binding site 1 out of 6 in 3awy

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Copper binding site 1 out of 6 in the Crystal Structure of Streptomyces Tyrosinase in A Complex with Caddie M84L 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 M84L 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:17.2
occ:0.45
CU A:CU500 0.0 17.2 0.5
CU A:CU500 1.0 21.2 0.5
NE2 A:HIS38 1.9 17.3 1.0
NE2 A:HIS63 1.9 15.7 1.0
NE2 A:HIS54 2.1 19.2 1.0
CD2 A:HIS38 2.7 17.0 1.0
O A:HOH509 2.7 18.1 0.5
CE1 A:HIS63 2.7 12.4 1.0
O B:HOH537 2.8 18.9 1.0
CE1 A:HIS54 2.9 18.5 1.0
CE1 A:HIS38 3.0 18.7 1.0
CD2 A:HIS63 3.1 14.0 1.0
CD2 A:HIS54 3.1 21.4 1.0
CG A:HIS38 3.9 15.7 1.0
ND1 A:HIS63 3.9 12.7 1.0
ND1 A:HIS38 4.0 16.9 1.0
CU A:CU501 4.1 15.2 1.0
ND1 A:HIS54 4.1 16.1 1.0
CG A:HIS63 4.1 12.9 1.0
CG A:HIS54 4.2 17.6 1.0
CZ A:PHE212 4.2 12.2 1.0
NE2 A:HIS216 4.3 15.0 1.0
CZ3 A:TRP62 4.4 13.8 1.0
CE2 A:PHE212 4.5 10.7 1.0
OH B:TYR98 4.5 17.8 1.0
CE1 A:HIS216 4.5 14.2 1.0
CD1 A:ILE42 4.9 23.8 1.0
O A:GLY53 4.9 16.7 1.0
CE3 A:TRP62 4.9 13.2 1.0

Copper binding site 2 out of 6 in 3awy

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Copper binding site 2 out of 6 in the Crystal Structure of Streptomyces Tyrosinase in A Complex with Caddie M84L 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 M84L 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:21.2
occ:0.47
CU A:CU500 0.0 21.2 0.5
CU A:CU500 1.0 17.2 0.5
O B:HOH537 1.9 18.9 1.0
O A:HOH509 1.9 18.1 0.5
NE2 A:HIS38 2.1 17.3 1.0
NE2 A:HIS54 2.3 19.2 1.0
NE2 A:HIS63 2.5 15.7 1.0
CE1 A:HIS38 2.9 18.7 1.0
CD2 A:HIS54 3.1 21.4 1.0
CU A:CU501 3.2 15.2 1.0
CD2 A:HIS38 3.3 17.0 1.0
CE1 A:HIS63 3.3 12.4 1.0
CE1 A:HIS54 3.4 18.5 1.0
CD2 A:HIS63 3.6 14.0 1.0
OH B:TYR98 3.7 17.8 1.0
NE2 A:HIS216 3.8 15.0 1.0
ND1 A:HIS38 4.2 16.9 1.0
CE1 A:HIS216 4.2 14.2 1.0
CE2 A:PHE212 4.3 10.7 1.0
CZ A:PHE212 4.3 12.2 1.0
CG A:HIS54 4.3 17.6 1.0
CG A:HIS38 4.3 15.7 1.0
CE2 B:TYR98 4.3 15.9 1.0
CD1 A:ILE42 4.4 23.8 1.0
ND1 A:HIS54 4.4 16.1 1.0
ND1 A:HIS63 4.5 12.7 1.0
CZ B:TYR98 4.5 15.5 1.0
NE2 A:HIS190 4.5 13.6 1.0
CG A:HIS63 4.7 12.9 1.0
NE2 A:HIS194 4.7 13.9 1.0
CD2 A:HIS216 4.8 13.0 1.0
CE1 A:PHE59 4.9 12.9 1.0
CE1 A:HIS190 5.0 15.9 1.0

Copper binding site 3 out of 6 in 3awy

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Copper binding site 3 out of 6 in the Crystal Structure of Streptomyces Tyrosinase in A Complex with Caddie M84L 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 M84L Mutant Soaked in A Cu(II)-Containing Solution For 80 Hr within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu501

b:15.2
occ:0.97
O B:HOH537 2.0 18.9 1.0
NE2 A:HIS190 2.0 13.6 1.0
NE2 A:HIS216 2.1 15.0 1.0
NE2 A:HIS194 2.1 13.9 1.0
O A:HOH509 2.3 18.1 0.5
CE1 A:HIS216 2.9 14.2 1.0
CE1 A:HIS190 3.0 15.9 1.0
CD2 A:HIS190 3.0 12.9 1.0
CE1 A:HIS194 3.0 12.8 1.0
CD2 A:HIS194 3.1 12.3 1.0
CU A:CU500 3.2 21.2 0.5
CD2 A:HIS216 3.2 13.0 1.0
CE2 B:TYR98 3.8 15.9 1.0
OH B:TYR98 3.9 17.8 1.0
CU A:CU500 4.1 17.2 0.5
ND1 A:HIS190 4.1 12.9 1.0
ND1 A:HIS216 4.1 13.5 1.0
CZ B:TYR98 4.1 15.5 1.0
CG A:HIS190 4.1 13.5 1.0
ND1 A:HIS194 4.2 12.1 1.0
CG A:HIS194 4.2 12.4 1.0
CG A:HIS216 4.2 12.2 1.0
CE2 A:PHE212 4.3 10.7 1.0
NE2 A:HIS63 4.4 15.7 1.0
CD2 A:HIS215 4.6 15.0 1.0
CD2 B:TYR98 4.7 13.5 1.0
NE2 A:HIS215 4.7 12.1 1.0
CE1 A:PHE59 4.8 12.9 1.0
NE2 A:HIS38 4.8 17.3 1.0
CD2 A:HIS63 4.8 14.0 1.0
CZ A:PHE212 4.9 12.2 1.0

Copper binding site 4 out of 6 in 3awy

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Copper binding site 4 out of 6 in the Crystal Structure of Streptomyces Tyrosinase in A Complex with Caddie M84L 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 4 of Crystal Structure of Streptomyces Tyrosinase in A Complex with Caddie M84L Mutant Soaked in A Cu(II)-Containing Solution For 80 Hr within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu503

b:42.0
occ:0.50
NE2 A:HIS277 1.9 38.4 1.0
NE2 A:HIS279 2.6 84.8 1.0
O A:HOH663 2.6 32.9 0.5
CE1 A:HIS277 2.8 38.3 1.0
CD2 A:HIS277 3.0 41.2 1.0
CD2 A:HIS279 3.3 85.1 1.0
CE1 A:HIS279 3.7 84.5 1.0
ND1 A:HIS277 4.0 39.9 1.0
CG A:HIS277 4.1 43.6 1.0
CG A:HIS279 4.6 85.2 1.0
ND1 A:HIS279 4.7 84.6 1.0
CG A:PRO231 4.7 29.9 1.0

Copper binding site 5 out of 6 in 3awy

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Copper binding site 5 out of 6 in the Crystal Structure of Streptomyces Tyrosinase in A Complex with Caddie M84L 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 5 of Crystal Structure of Streptomyces Tyrosinase in A Complex with Caddie M84L Mutant Soaked in A Cu(II)-Containing Solution For 80 Hr within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu504

b:64.0
occ:0.51
NE2 A:HIS180 2.0 20.4 1.0
CD2 A:HIS180 3.0 18.5 1.0
CE1 A:HIS180 3.0 21.3 1.0
O A:HOH639 3.7 29.0 1.0
CA A:GLY186 3.9 17.3 1.0
OE2 A:GLU175 3.9 43.7 1.0
ND1 A:HIS180 4.1 20.8 1.0
CG A:HIS180 4.1 16.9 1.0
N A:GLY186 4.3 19.5 1.0
O A:HOH756 4.3 46.0 1.0
OE1 A:GLU175 4.5 49.6 1.0
CD A:GLU175 4.6 37.3 1.0
C A:ARG185 4.8 19.3 1.0

Copper binding site 6 out of 6 in 3awy

Go back to Copper Binding Sites List in 3awy
Copper binding site 6 out of 6 in the Crystal Structure of Streptomyces Tyrosinase in A Complex with Caddie M84L 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 6 of Crystal Structure of Streptomyces Tyrosinase in A Complex with Caddie M84L Mutant Soaked in A Cu(II)-Containing Solution For 80 Hr within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu502

b:46.6
occ:0.80
NE2 B:HIS82 2.1 30.4 1.0
CD2 B:HIS82 2.8 27.1 1.0
CE1 B:HIS82 3.2 27.2 1.0
O A:HOH760 3.6 50.5 1.0
CG B:HIS82 4.0 25.5 1.0
ND1 B:HIS82 4.2 24.7 1.0
O A:MET43 4.2 28.8 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 01:57:12 2025

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