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Copper in PDB 3awx: Crystal Structure of Streptomyces Tyrosinase in A Complex with Caddie H82Q Mutant Soaked in A Cu(II)-Containing Solution For 80 Hr

Enzymatic activity of Crystal Structure of Streptomyces Tyrosinase in A Complex with Caddie H82Q 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 H82Q 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 H82Q Mutant Soaked in A Cu(II)-Containing Solution For 80 Hr, PDB code: 3awx 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 / 1.25
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 65.010, 97.490, 54.890, 90.00, 90.00, 90.00
R / Rfree (%) 13.8 / 18.4

Copper Binding Sites:

The binding sites of Copper atom in the Crystal Structure of Streptomyces Tyrosinase in A Complex with Caddie H82Q Mutant Soaked in A Cu(II)-Containing Solution For 80 Hr (pdb code 3awx). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 7 binding sites of Copper where determined in the Crystal Structure of Streptomyces Tyrosinase in A Complex with Caddie H82Q Mutant Soaked in A Cu(II)-Containing Solution For 80 Hr, PDB code: 3awx:
Jump to Copper binding site number: 1; 2; 3; 4; 5; 6; 7;

Copper binding site 1 out of 7 in 3awx

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Copper binding site 1 out of 7 in the Crystal Structure of Streptomyces Tyrosinase in A Complex with Caddie H82Q 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 H82Q 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:9.0
occ:0.48
 CU A:CU500 0.0 9.0 0.5
CU A:CU500 1.2 15.0 0.5
O A:HOH511 1.9 13.5 0.8
O B:HOH529 2.0 11.9 1.0
NE2 A:HIS54 2.0 13.3 1.0
NE2 A:HIS38 2.1 12.4 1.0
NE2 A:HIS63 2.6 10.3 1.0
CD2 A:HIS54 2.9 12.1 1.0
CE1 A:HIS38 3.0 10.9 1.0
CE1 A:HIS54 3.1 11.8 1.0
CD2 A:HIS38 3.2 12.8 1.0
CU A:CU501 3.3 11.2 0.9
CE1 A:HIS63 3.3 9.7 1.0
OH B:TYR98 3.7 10.5 1.0
CD2 A:HIS63 3.7 8.9 1.0
NE2 A:HIS216 4.0 7.9 1.0
CG A:HIS54 4.1 10.8 1.0
ND1 A:HIS38 4.2 10.1 1.0
ND1 A:HIS54 4.2 11.0 1.0
CE2 B:TYR98 4.3 9.9 1.0
CG A:HIS38 4.3 11.4 1.0
CD1 A:ILE42 4.3 14.9 1.0
CE2 A:PHE212 4.5 10.1 1.0
CE1 A:HIS216 4.5 8.1 1.0
CZ B:TYR98 4.5 9.9 1.0
ND1 A:HIS63 4.5 8.9 1.0
CZ A:PHE212 4.5 9.6 1.0
NE2 A:HIS190 4.6 8.5 1.0
CG A:HIS63 4.7 8.2 1.0
NE2 A:HIS194 4.9 7.7 1.0
CE1 A:PHE59 4.9 9.7 1.0
CG1 A:ILE42 5.0 12.9 1.0

Copper binding site 2 out of 7 in 3awx

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Copper binding site 2 out of 7 in the Crystal Structure of Streptomyces Tyrosinase in A Complex with Caddie H82Q 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 H82Q 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:15.0
occ:0.47
 CU A:CU500 0.0 15.0 0.5
CU A:CU500 1.2 9.0 0.5
NE2 A:HIS38 1.8 12.4 1.0
NE2 A:HIS63 1.9 10.3 1.0
NE2 A:HIS54 2.1 13.3 1.0
CD2 A:HIS38 2.5 12.8 1.0
CE1 A:HIS63 2.7 9.7 1.0
CE1 A:HIS54 2.8 11.8 1.0
O A:HOH511 2.8 13.5 0.8
O B:HOH529 2.9 11.9 1.0
CD2 A:HIS63 3.0 8.9 1.0
CE1 A:HIS38 3.1 10.9 1.0
CD2 A:HIS54 3.3 12.1 1.0
CG A:HIS38 3.8 11.4 1.0
ND1 A:HIS63 3.9 8.9 1.0
ND1 A:HIS38 4.0 10.1 1.0
ND1 A:HIS54 4.0 11.0 1.0
CG A:HIS63 4.1 8.2 1.0
CU A:CU501 4.2 11.2 0.9
CZ A:PHE212 4.3 9.6 1.0
CG A:HIS54 4.3 10.8 1.0
CZ3 A:TRP62 4.3 10.6 1.0
NE2 A:HIS216 4.4 7.9 1.0
CE2 A:PHE212 4.5 10.1 1.0
OH B:TYR98 4.6 10.5 1.0
CE1 A:HIS216 4.7 8.1 1.0
CE3 A:TRP62 4.9 9.1 1.0
O A:GLY53 4.9 10.4 1.0

Copper binding site 3 out of 7 in 3awx

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Copper binding site 3 out of 7 in the Crystal Structure of Streptomyces Tyrosinase in A Complex with Caddie H82Q 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 H82Q 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:11.2
occ:0.94
 O B:HOH529 1.9 11.9 1.0
NE2 A:HIS190 2.0 8.5 1.0
NE2 A:HIS194 2.1 7.7 1.0
NE2 A:HIS216 2.1 7.9 1.0
O A:HOH511 2.2 13.5 0.8
CE1 A:HIS190 2.9 8.8 1.0
CE1 A:HIS194 3.0 8.1 1.0
CE1 A:HIS216 3.0 8.1 1.0
CD2 A:HIS190 3.0 7.9 1.0
CD2 A:HIS194 3.1 8.2 1.0
CD2 A:HIS216 3.2 7.9 1.0
CU A:CU500 3.3 9.0 0.5
CE2 B:TYR98 3.7 9.9 1.0
OH B:TYR98 3.9 10.5 1.0
CZ B:TYR98 4.1 9.9 1.0
ND1 A:HIS190 4.1 8.6 1.0
ND1 A:HIS194 4.1 8.2 1.0
CG A:HIS190 4.2 8.2 1.0
CU A:CU500 4.2 15.0 0.5
CG A:HIS194 4.2 8.2 1.0
ND1 A:HIS216 4.2 7.8 1.0
CG A:HIS216 4.3 7.7 1.0
CE2 A:PHE212 4.4 10.1 1.0
NE2 A:HIS63 4.4 10.3 1.0
CD2 B:TYR98 4.6 9.9 1.0
CD2 A:HIS215 4.7 9.0 1.0
CE1 A:PHE59 4.7 9.7 1.0
NE2 A:HIS38 4.8 12.4 1.0
NE2 A:HIS215 4.8 8.7 1.0
CD2 A:HIS63 4.9 8.9 1.0
CZ A:PHE212 4.9 9.6 1.0
NE2 A:HIS54 5.0 13.3 1.0

Copper binding site 4 out of 7 in 3awx

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Copper binding site 4 out of 7 in the Crystal Structure of Streptomyces Tyrosinase in A Complex with Caddie H82Q 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 H82Q 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:22.7
occ:0.50
 NE2 A:HIS277 2.0 21.6 1.0
NE2 A:HIS279 2.1 37.9 1.0
O A:HOH614 2.4 21.0 0.5
CE1 A:HIS277 3.0 20.9 1.0
CD2 A:HIS277 3.0 22.3 1.0
CE1 A:HIS279 3.1 37.9 1.0
CD2 A:HIS279 3.1 39.0 1.0
ND1 A:HIS277 4.1 21.0 1.0
CG A:HIS277 4.1 22.6 1.0
ND1 A:HIS279 4.2 39.2 1.0
CG A:HIS279 4.2 40.3 1.0
O A:HOH694 4.6 27.5 1.0
CG A:PRO231 4.6 19.9 1.0

Copper binding site 5 out of 7 in 3awx

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Copper binding site 5 out of 7 in the Crystal Structure of Streptomyces Tyrosinase in A Complex with Caddie H82Q 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 H82Q 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:63.9
occ:0.37
 NE2 A:HIS276 2.5 46.5 1.0
CD2 A:HIS276 3.2 45.1 1.0
CE1 A:HIS276 3.6 45.9 1.0
CG A:HIS276 4.5 43.7 1.0
ND1 A:HIS276 4.6 45.4 1.0

Copper binding site 6 out of 7 in 3awx

Go back to Copper Binding Sites List in 3awx
Copper binding site 6 out of 7 in the Crystal Structure of Streptomyces Tyrosinase in A Complex with Caddie H82Q 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 H82Q Mutant Soaked in A Cu(II)-Containing Solution For 80 Hr within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu505

b:42.5
occ:0.25
 NE2 A:HIS278 2.2 48.7 1.0
CE1 A:HIS278 3.0 48.5 1.0
CD2 A:HIS278 3.4 47.4 1.0
OE1 A:GLU275 4.0 48.7 1.0
ND1 A:HIS278 4.2 47.5 1.0
CG A:HIS278 4.4 45.5 1.0

Copper binding site 7 out of 7 in 3awx

Go back to Copper Binding Sites List in 3awx
Copper binding site 7 out of 7 in the Crystal Structure of Streptomyces Tyrosinase in A Complex with Caddie H82Q 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 7 of Crystal Structure of Streptomyces Tyrosinase in A Complex with Caddie H82Q Mutant Soaked in A Cu(II)-Containing Solution For 80 Hr within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu503

b:44.6
occ:0.28
 O1 A:NO3510 1.7 43.4 0.7
N A:NO3510 1.7 43.5 0.7
NE2 B:HIS97 1.9 20.5 1.0
O3 A:NO3510 2.2 43.9 0.7
O2 A:NO3510 2.2 43.4 0.7
CE1 B:HIS97 2.3 19.4 1.0
CE B:MET84 2.8 25.8 1.0
O A:ILE42 2.9 14.0 1.0
CA A:MET43 3.0 18.2 1.0
CD2 B:HIS97 3.2 19.2 1.0
C A:ILE42 3.5 13.3 1.0
N A:MET43 3.6 13.9 1.0
ND1 B:HIS97 3.6 16.3 1.0
CB A:MET43 3.8 18.9 1.0
C A:MET43 3.8 18.3 1.0
O A:MET43 3.8 22.7 1.0
CG A:MET43 3.8 21.3 1.0
CD1 B:ILE92 4.0 23.1 1.0
CG B:HIS97 4.1 16.0 1.0
SD B:MET84 4.1 23.9 1.0
CB B:MET84 4.6 17.4 1.0
O A:HOH563 4.7 16.7 1.0
CG2 A:ILE42 4.8 14.1 1.0
CA A:ILE42 4.9 11.7 1.0
N A:SER44 4.9 16.6 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 01:57:03 2025

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