Atomistry » Copper » PDB 1tmx-1x9l » 1wx2
Atomistry »
  Copper »
    PDB 1tmx-1x9l »
      1wx2 »

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

Go back to Copper Binding Sites List in 1wx2
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

Go back to Copper Binding Sites List in 1wx2
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

Go back to Copper Binding Sites List in 1wx2
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

Go back to Copper Binding Sites List in 1wx2
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: Tue Jul 30 22:59:56 2024

Last articles

Zn in 9J0N
Zn in 9J0O
Zn in 9J0P
Zn in 9FJX
Zn in 9EKB
Zn in 9C0F
Zn in 9CAH
Zn in 9CH0
Zn in 9CH3
Zn in 9CH1
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy