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Copper in PDB 1wx2: Crystal Structure of the Oxy-Form of the Copper-Bound Streptomyces Castaneoglobisporus Tyrosinase Complexed with A Caddie Protein Prepared By the Addition of Hydrogenperoxide

Enzymatic activity of Crystal Structure of the Oxy-Form of the Copper-Bound Streptomyces Castaneoglobisporus Tyrosinase Complexed with A Caddie Protein Prepared By the Addition of Hydrogenperoxide

All present enzymatic activity of Crystal Structure of the Oxy-Form of the Copper-Bound Streptomyces Castaneoglobisporus Tyrosinase Complexed with A Caddie Protein Prepared By the Addition of Hydrogenperoxide:
1.14.18.1;

Protein crystallography data

The structure of Crystal Structure of the Oxy-Form of the Copper-Bound Streptomyces Castaneoglobisporus Tyrosinase Complexed with A Caddie Protein Prepared By the Addition of Hydrogenperoxide, PDB code: 1wx2 was solved by Y.Matoba, T.Kumagai, A.Yamamoto, H.Yoshitsu, M.Sugiyama, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.00 / 1.80
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 65.160, 96.550, 54.720, 90.00, 90.00, 90.00
R / Rfree (%) 21 / 24.9

Copper Binding Sites:

The binding sites of Copper atom in the Crystal Structure of the Oxy-Form of the Copper-Bound Streptomyces Castaneoglobisporus Tyrosinase Complexed with A Caddie Protein Prepared By the Addition of Hydrogenperoxide (pdb code 1wx2). 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 the Oxy-Form of the Copper-Bound Streptomyces Castaneoglobisporus Tyrosinase Complexed with A Caddie Protein Prepared By the Addition of Hydrogenperoxide, PDB code: 1wx2:
Jump to Copper binding site number: 1; 2; 3; 4; 5;

Copper binding site 1 out of 5 in 1wx2

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Copper binding site 1 out of 5 in the Crystal Structure of the Oxy-Form of the Copper-Bound Streptomyces Castaneoglobisporus Tyrosinase Complexed with A Caddie Protein Prepared By the Addition of Hydrogenperoxide


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 the Oxy-Form of the Copper-Bound Streptomyces Castaneoglobisporus Tyrosinase Complexed with A Caddie Protein Prepared By the Addition of Hydrogenperoxide within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu400

b:37.4
occ:1.00
 O2 A:PER404 1.9 28.2 1.0
O1 A:PER404 2.0 25.6 1.0
NE2 A:HIS38 2.1 27.2 1.0
NE2 A:HIS54 2.2 34.2 1.0
NE2 A:HIS63 2.2 21.1 1.0
CE1 A:HIS63 2.9 18.1 1.0
CD2 A:HIS54 3.0 32.7 1.0
CD2 A:HIS38 3.0 22.4 1.0
CE1 A:HIS38 3.2 25.0 1.0
CE1 A:HIS54 3.3 27.9 1.0
CD2 A:HIS63 3.4 20.0 1.0
CU A:CU401 3.5 24.6 1.0
NE2 A:HIS216 4.0 17.9 1.0
CD1 A:ILE42 4.1 30.7 1.0
ND1 A:HIS63 4.1 20.9 1.0
CG A:HIS54 4.2 31.9 1.0
CG A:HIS38 4.2 25.1 1.0
ND1 A:HIS38 4.3 23.5 1.0
CE1 A:HIS216 4.3 13.7 1.0
ND1 A:HIS54 4.3 26.7 1.0
CG A:HIS63 4.4 20.2 1.0
OH B:TYR98 4.4 21.6 1.0
CE2 A:PHE212 4.4 16.3 1.0
CZ A:PHE212 4.6 19.2 1.0
NE2 A:HIS190 4.9 25.3 1.0
CE1 A:PHE59 4.9 17.3 1.0
CD2 A:HIS216 5.0 16.0 1.0

Copper binding site 2 out of 5 in 1wx2

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Copper binding site 2 out of 5 in the Crystal Structure of the Oxy-Form of the Copper-Bound Streptomyces Castaneoglobisporus Tyrosinase Complexed with A Caddie Protein Prepared By the Addition of Hydrogenperoxide


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 the Oxy-Form of the Copper-Bound Streptomyces Castaneoglobisporus Tyrosinase Complexed with A Caddie Protein Prepared By the Addition of Hydrogenperoxide within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu401

b:24.6
occ:1.00
 O2 A:PER404 1.9 28.2 1.0
NE2 A:HIS194 2.1 18.2 1.0
NE2 A:HIS190 2.1 25.3 1.0
O1 A:PER404 2.1 25.6 1.0
NE2 A:HIS216 2.1 17.9 1.0
CE1 A:HIS190 3.0 19.9 1.0
CE1 A:HIS194 3.0 18.6 1.0
CE1 A:HIS216 3.0 13.7 1.0
CD2 A:HIS194 3.1 12.9 1.0
CD2 A:HIS190 3.2 19.6 1.0
CD2 A:HIS216 3.3 16.0 1.0
CU A:CU400 3.5 37.4 1.0
CE2 B:TYR98 4.0 24.3 1.0
ND1 A:HIS194 4.1 18.4 1.0
ND1 A:HIS190 4.1 20.9 1.0
ND1 A:HIS216 4.2 16.7 1.0
CG A:HIS194 4.2 17.3 1.0
CG A:HIS190 4.2 20.7 1.0
OH B:TYR98 4.3 21.6 1.0
CG A:HIS216 4.3 17.9 1.0
CZ B:TYR98 4.4 23.6 1.0
NE2 A:HIS63 4.5 21.1 1.0
CE2 A:PHE212 4.5 16.3 1.0
NE2 A:HIS215 4.7 20.6 1.0
CD2 A:HIS215 4.7 20.3 1.0
CE1 A:PHE59 4.8 17.3 1.0
CD2 B:TYR98 4.8 21.2 1.0
NE2 A:HIS38 4.8 27.2 1.0
CD2 A:HIS63 4.9 20.0 1.0

Copper binding site 3 out of 5 in 1wx2

Go back to Copper Binding Sites List in 1wx2
Copper binding site 3 out of 5 in the Crystal Structure of the Oxy-Form of the Copper-Bound Streptomyces Castaneoglobisporus Tyrosinase Complexed with A Caddie Protein Prepared By the Addition of Hydrogenperoxide


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 the Oxy-Form of the Copper-Bound Streptomyces Castaneoglobisporus Tyrosinase Complexed with A Caddie Protein Prepared By the Addition of Hydrogenperoxide within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu403

b:67.7
occ:1.00
 NE2 A:HIS180 2.2 40.7 1.0
CD2 A:HIS180 3.1 29.3 1.0
CE1 A:HIS180 3.2 34.1 1.0
OE2 A:GLU175 3.3 40.6 1.0
OE1 A:GLU175 3.9 42.7 1.0
CD A:GLU175 4.0 38.4 1.0
O A:HOH567 4.2 31.4 1.0
CG A:HIS180 4.3 29.6 1.0
ND1 A:HIS180 4.3 31.1 1.0
CA A:GLY186 4.3 22.0 1.0
N A:GLY186 4.6 26.3 1.0
O A:HOH453 4.9 40.5 1.0
C A:ARG185 4.9 26.3 1.0

Copper binding site 4 out of 5 in 1wx2

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Copper binding site 4 out of 5 in the Crystal Structure of the Oxy-Form of the Copper-Bound Streptomyces Castaneoglobisporus Tyrosinase Complexed with A Caddie Protein Prepared By the Addition of Hydrogenperoxide


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 the Oxy-Form of the Copper-Bound Streptomyces Castaneoglobisporus Tyrosinase Complexed with A Caddie Protein Prepared By the Addition of Hydrogenperoxide within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu402

b:49.6
occ:0.50
 NE2 B:HIS82 2.1 40.7 0.5
CE1 B:HIS82 2.9 32.0 0.5
CD2 B:HIS82 2.9 37.0 0.5
ND1 B:HIS82 3.2 33.9 0.5
CE1 B:HIS82 3.2 35.6 0.5
O A:MET43 4.0 33.0 1.0
CG B:HIS82 4.1 35.5 0.5
NE2 B:HIS82 4.2 30.6 0.5
ND1 B:HIS82 4.3 34.7 0.5
CG B:HIS82 4.5 32.5 0.5
O B:HOH562 4.8 30.0 1.0
C A:MET43 5.0 32.0 1.0

Copper binding site 5 out of 5 in 1wx2

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Copper binding site 5 out of 5 in the Crystal Structure of the Oxy-Form of the Copper-Bound Streptomyces Castaneoglobisporus Tyrosinase Complexed with A Caddie Protein Prepared By the Addition of Hydrogenperoxide


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 the Oxy-Form of the Copper-Bound Streptomyces Castaneoglobisporus Tyrosinase Complexed with A Caddie Protein Prepared By the Addition of Hydrogenperoxide within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu402

b:35.5
occ:0.50
 O B:HOH644 2.3 22.6 0.5
CE1 B:HIS97 2.3 35.1 0.5
NE2 B:HIS82 2.4 30.6 0.5
NE2 B:HIS97 2.5 34.0 0.5
SD B:MET84 2.8 37.1 1.0
CD2 B:HIS82 3.0 31.7 0.5
CG B:MET84 3.0 33.5 1.0
NE2 B:HIS97 3.1 34.9 0.5
CD2 B:HIS97 3.3 32.9 0.5
ND1 B:HIS82 3.3 34.7 0.5
O A:ILE42 3.3 30.4 1.0
CE1 B:HIS82 3.3 35.6 0.5
ND1 B:HIS97 3.4 33.7 0.5
CB B:MET84 3.4 28.5 1.0
CE1 B:HIS97 3.6 34.4 0.5
CE1 B:HIS82 3.7 32.0 0.5
CA A:MET43 3.9 32.5 1.0
O A:MET43 4.0 33.0 1.0
CG B:HIS82 4.3 32.5 0.5
C A:ILE42 4.3 31.4 1.0
C A:MET43 4.3 32.0 1.0
CD2 B:HIS97 4.4 34.4 0.5
CG B:HIS97 4.5 32.6 0.5
CG B:HIS97 4.5 32.2 0.5
CE B:MET84 4.5 40.1 1.0
N A:MET43 4.5 30.4 1.0
ND1 B:HIS82 4.6 33.9 0.5
CA B:MET84 4.6 24.6 1.0
N B:MET84 4.6 24.5 1.0
ND1 B:HIS97 4.6 34.0 0.5
NE2 B:HIS82 4.7 40.7 0.5
CG B:HIS82 4.7 35.5 0.5
C B:VAL83 4.7 22.4 1.0
O A:HOH617 4.7 24.8 1.0
CG A:MET43 4.8 35.2 1.0
O B:VAL83 4.8 21.8 1.0
CB A:MET43 4.8 33.8 1.0
CD1 B:ILE92 4.9 25.7 1.0

Reference:

Y.Matoba, T.Kumagai, A.Yamamoto, H.Yoshitsu, M.Sugiyama. Crystallographic Evidence That the Dinuclear Copper Center of Tyrosinase Is Flexible During Catalysis J.Biol.Chem. V. 281 8981 2006.
ISSN: ISSN 0021-9258
PubMed: 16436386
DOI: 10.1074/JBC.M509785200
Page generated: Mon Jul 14 00:36:26 2025

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