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Copper in PDB 2ahk: Crystal Structure of the Met-Form of the Copper-Bound Streptomyces Castaneoglobisporus Tyrosinase in Complex with A Caddie Protein Obtained By Soking in Cupric Sulfate For 6 Months

Enzymatic activity of Crystal Structure of the Met-Form of the Copper-Bound Streptomyces Castaneoglobisporus Tyrosinase in Complex with A Caddie Protein Obtained By Soking in Cupric Sulfate For 6 Months

All present enzymatic activity of Crystal Structure of the Met-Form of the Copper-Bound Streptomyces Castaneoglobisporus Tyrosinase in Complex with A Caddie Protein Obtained By Soking in Cupric Sulfate For 6 Months:
1.14.18.1;

Protein crystallography data

The structure of Crystal Structure of the Met-Form of the Copper-Bound Streptomyces Castaneoglobisporus Tyrosinase in Complex with A Caddie Protein Obtained By Soking in Cupric Sulfate For 6 Months, PDB code: 2ahk 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 / 1.71
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 65.100, 97.470, 54.830, 90.00, 90.00, 90.00
R / Rfree (%) 19.4 / 24.1

Copper Binding Sites:

The binding sites of Copper atom in the Crystal Structure of the Met-Form of the Copper-Bound Streptomyces Castaneoglobisporus Tyrosinase in Complex with A Caddie Protein Obtained By Soking in Cupric Sulfate For 6 Months (pdb code 2ahk). 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 the Met-Form of the Copper-Bound Streptomyces Castaneoglobisporus Tyrosinase in Complex with A Caddie Protein Obtained By Soking in Cupric Sulfate For 6 Months, PDB code: 2ahk:
Jump to Copper binding site number: 1; 2; 3;

Copper binding site 1 out of 3 in 2ahk

Go back to Copper Binding Sites List in 2ahk
Copper binding site 1 out of 3 in the Crystal Structure of the Met-Form of the Copper-Bound Streptomyces Castaneoglobisporus Tyrosinase in Complex with A Caddie Protein Obtained By Soking in Cupric Sulfate For 6 Months


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 Met-Form of the Copper-Bound Streptomyces Castaneoglobisporus Tyrosinase in Complex with A Caddie Protein Obtained By Soking in Cupric Sulfate For 6 Months within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu400

b:30.1
occ:1.00
 NE2 A:HIS38 2.1 17.8 1.0
O B:HOH411 2.2 27.4 1.0
NE2 A:HIS54 2.3 25.1 1.0
O A:HOH410 2.4 28.3 1.0
NE2 A:HIS63 2.4 15.8 1.0
CD2 A:HIS54 3.0 20.9 1.0
CD2 A:HIS38 3.0 15.4 1.0
CE1 A:HIS63 3.1 10.9 1.0
CE1 A:HIS38 3.1 16.6 1.0
CU A:CU401 3.3 22.6 1.0
CE1 A:HIS54 3.4 24.1 1.0
CD2 A:HIS63 3.6 15.6 1.0
OH B:TYR98 3.8 25.2 1.0
NE2 A:HIS216 4.1 18.5 1.0
CG A:HIS38 4.2 16.2 1.0
ND1 A:HIS38 4.2 16.1 1.0
CG A:HIS54 4.2 23.4 1.0
CD1 A:ILE42 4.3 24.5 1.0
ND1 A:HIS63 4.3 13.5 1.0
ND1 A:HIS54 4.4 24.0 1.0
CE2 A:PHE212 4.4 14.2 1.0
CE1 A:HIS216 4.4 18.2 1.0
CE2 B:TYR98 4.5 21.3 1.0
CG A:HIS63 4.6 18.4 1.0
CZ B:TYR98 4.6 20.4 1.0
CZ A:PHE212 4.6 15.1 1.0
NE2 A:HIS190 4.9 19.5 1.0
CE1 A:PHE59 4.9 16.9 1.0
NE2 A:HIS194 5.0 18.7 1.0

Copper binding site 2 out of 3 in 2ahk

Go back to Copper Binding Sites List in 2ahk
Copper binding site 2 out of 3 in the Crystal Structure of the Met-Form of the Copper-Bound Streptomyces Castaneoglobisporus Tyrosinase in Complex with A Caddie Protein Obtained By Soking in Cupric Sulfate For 6 Months


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 Met-Form of the Copper-Bound Streptomyces Castaneoglobisporus Tyrosinase in Complex with A Caddie Protein Obtained By Soking in Cupric Sulfate For 6 Months within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu401

b:22.6
occ:1.00
 O A:HOH410 2.0 28.3 1.0
O B:HOH411 2.0 27.4 1.0
NE2 A:HIS190 2.0 19.5 1.0
NE2 A:HIS194 2.2 18.7 1.0
NE2 A:HIS216 2.2 18.5 1.0
CE1 A:HIS190 2.9 18.0 1.0
CE1 A:HIS216 2.9 18.2 1.0
CE1 A:HIS194 3.1 16.0 1.0
CD2 A:HIS194 3.1 17.2 1.0
CD2 A:HIS190 3.2 18.4 1.0
CU A:CU400 3.3 30.1 1.0
CD2 A:HIS216 3.3 15.5 1.0
CE2 B:TYR98 3.7 21.3 1.0
OH B:TYR98 3.9 25.2 1.0
ND1 A:HIS190 4.1 19.0 1.0
CZ B:TYR98 4.1 20.4 1.0
ND1 A:HIS216 4.1 16.9 1.0
ND1 A:HIS194 4.2 16.8 1.0
CG A:HIS190 4.2 19.0 1.0
CG A:HIS194 4.2 17.1 1.0
NE2 A:HIS63 4.4 15.8 1.0
CG A:HIS216 4.4 17.2 1.0
CE2 A:PHE212 4.5 14.2 1.0
CD2 B:TYR98 4.6 19.0 1.0
CE1 A:PHE59 4.6 16.9 1.0
NE2 A:HIS38 4.8 17.8 1.0
CD2 A:HIS215 4.8 19.0 1.0
CD2 A:HIS63 4.8 15.6 1.0
NE2 A:HIS215 4.8 19.4 1.0
CZ A:PHE59 5.0 16.1 1.0
CE1 A:HIS63 5.0 10.9 1.0

Copper binding site 3 out of 3 in 2ahk

Go back to Copper Binding Sites List in 2ahk
Copper binding site 3 out of 3 in the Crystal Structure of the Met-Form of the Copper-Bound Streptomyces Castaneoglobisporus Tyrosinase in Complex with A Caddie Protein Obtained By Soking in Cupric Sulfate For 6 Months


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 Met-Form of the Copper-Bound Streptomyces Castaneoglobisporus Tyrosinase in Complex with A Caddie Protein Obtained By Soking in Cupric Sulfate For 6 Months within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu402

b:41.4
occ:1.00
 NE2 B:HIS97 2.2 34.4 1.0
NE2 B:HIS82 2.2 31.4 1.0
SD B:MET84 2.5 35.1 1.0
CE1 B:HIS97 3.0 29.6 1.0
CD2 B:HIS82 3.1 29.6 1.0
CE1 B:HIS82 3.2 28.5 1.0
CG B:MET84 3.3 30.4 1.0
CD2 B:HIS97 3.3 27.8 1.0
O A:ILE42 3.4 25.3 1.0
CB B:MET84 3.5 23.7 1.0
CE B:MET84 3.6 33.6 1.0
CA A:MET43 3.8 30.3 1.0
O A:MET43 4.1 32.4 1.0
ND1 B:HIS97 4.1 26.8 1.0
C A:MET43 4.2 30.4 1.0
C A:ILE42 4.3 27.2 1.0
CG B:HIS82 4.3 26.7 1.0
ND1 B:HIS82 4.3 29.0 1.0
CG B:HIS97 4.4 26.9 1.0
N A:MET43 4.5 28.2 1.0
O A:HOH683 4.7 22.4 1.0
CB A:MET43 4.7 31.1 1.0
CG A:MET43 4.7 35.7 1.0
CA B:MET84 4.7 22.1 1.0
N B:MET84 4.7 20.7 1.0
CD1 B:ILE92 4.8 31.3 1.0
C B:VAL83 4.9 21.2 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 23:08:05 2024

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