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Copper in PDB 2ahl: Crystal Structure of the Hydroxylamine-Induced Deoxy-Form of the Copper-Bound Streptomyces Castaneoglobisporus Tyrosinase in Complex with A Caddie Protein
Enzymatic activity of Crystal Structure of the Hydroxylamine-Induced Deoxy-Form of the Copper-Bound Streptomyces Castaneoglobisporus Tyrosinase in Complex with A Caddie Protein
All present enzymatic activity of Crystal Structure of the Hydroxylamine-Induced Deoxy-Form of the Copper-Bound Streptomyces Castaneoglobisporus Tyrosinase in Complex with A Caddie Protein:
1.14.18.1;
1.14.18.1;
Protein crystallography data
The structure of Crystal Structure of the Hydroxylamine-Induced Deoxy-Form of the Copper-Bound Streptomyces Castaneoglobisporus Tyrosinase in Complex with A Caddie Protein, PDB code: 2ahl
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 / 1.60 |
| Space group | P 21 21 2 |
| Cell size a, b, c (Å), α, β, γ (°) | 65.470, 97.920, 55.160, 90.00, 90.00, 90.00 |
| R / Rfree (%) | 21.5 / 26.3 |
Copper Binding Sites:
The binding sites of Copper atom in the Crystal Structure of the Hydroxylamine-Induced Deoxy-Form of the Copper-Bound Streptomyces Castaneoglobisporus Tyrosinase in Complex with A Caddie Protein
(pdb code 2ahl). 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 Hydroxylamine-Induced Deoxy-Form of the Copper-Bound Streptomyces Castaneoglobisporus Tyrosinase in Complex with A Caddie Protein, PDB code: 2ahl:
Jump to Copper binding site number: 1; 2; 3;
In total 3 binding sites of Copper where determined in the Crystal Structure of the Hydroxylamine-Induced Deoxy-Form of the Copper-Bound Streptomyces Castaneoglobisporus Tyrosinase in Complex with A Caddie Protein, PDB code: 2ahl:
Jump to Copper binding site number: 1; 2; 3;
Copper binding site 1 out of 3 in 2ahl
Go back to
Copper Binding Sites List in 2ahl
Copper binding site 1 out
of 3 in the Crystal Structure of the Hydroxylamine-Induced Deoxy-Form of the Copper-Bound Streptomyces Castaneoglobisporus Tyrosinase in Complex with A Caddie Protein
Mono view
Stereo pair view
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 Hydroxylamine-Induced Deoxy-Form of the Copper-Bound Streptomyces Castaneoglobisporus Tyrosinase in Complex with A Caddie Protein within 5.0Å range:
|
Copper binding site 2 out of 3 in 2ahl
Go back to
Copper Binding Sites List in 2ahl
Copper binding site 2 out
of 3 in the Crystal Structure of the Hydroxylamine-Induced Deoxy-Form of the Copper-Bound Streptomyces Castaneoglobisporus Tyrosinase in Complex with A Caddie Protein
Mono view
Stereo pair view
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 Hydroxylamine-Induced Deoxy-Form of the Copper-Bound Streptomyces Castaneoglobisporus Tyrosinase in Complex with A Caddie Protein within 5.0Å range:
|
Copper binding site 3 out of 3 in 2ahl
Go back to
Copper Binding Sites List in 2ahl
Copper binding site 3 out
of 3 in the Crystal Structure of the Hydroxylamine-Induced Deoxy-Form of the Copper-Bound Streptomyces Castaneoglobisporus Tyrosinase in Complex with A Caddie Protein
Mono view
Stereo pair view
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 Hydroxylamine-Induced Deoxy-Form of the Copper-Bound Streptomyces Castaneoglobisporus Tyrosinase in Complex with A Caddie Protein within 5.0Å range:
|
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 23:08:08 2024
ISSN: ISSN 0021-9258
PubMed: 16436386
DOI: 10.1074/JBC.M509785200
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