Atomistry » Copper » PDB 1x9r-2ahl » 2ahk
Atomistry »
  Copper »
    PDB 1x9r-2ahl »
      2ahk »

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

Last articles

Zn in 9MJ5
Zn in 9HNW
Zn in 9G0L
Zn in 9FNE
Zn in 9DZN
Zn in 9E0I
Zn in 9D32
Zn in 9DAK
Zn in 8ZXC
Zn in 8ZUF
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy