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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;

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;

Copper binding site 1 out of 3 in 2ahl

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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

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:
probe atom residue distance (Å) B Occ
A:Cu400

b:28.6
occ:1.00
NE2 A:HIS63 2.0 13.3 1.0
NE2 A:HIS38 2.1 19.7 1.0
NE2 A:HIS54 2.2 22.4 1.0
O B:HOH411 2.4 10.7 1.0
CE1 A:HIS63 2.8 9.0 1.0
CD2 A:HIS38 2.8 15.6 1.0
CD2 A:HIS54 3.0 18.4 1.0
CD2 A:HIS63 3.2 10.4 1.0
CE1 A:HIS54 3.2 20.3 1.0
CE1 A:HIS38 3.3 18.0 1.0
ND1 A:HIS63 4.0 10.7 1.0
CG A:HIS38 4.0 15.7 1.0
CZ A:PHE212 4.1 10.9 1.0
CU A:CU1401 4.2 21.4 1.0
CG A:HIS54 4.2 18.4 1.0
ND1 A:HIS38 4.2 15.9 1.0
CG A:HIS63 4.2 10.4 1.0
NE2 A:HIS216 4.3 13.5 1.0
ND1 A:HIS54 4.3 18.2 1.0
CE2 A:PHE212 4.3 12.5 1.0
CD1 A:ILE42 4.3 23.4 1.0
CE1 A:HIS216 4.5 9.9 1.0
OH B:TYR98 4.5 16.1 1.0
CZ3 A:TRP62 4.5 14.4 1.0
O A:GLY53 5.0 11.4 1.0

Copper binding site 2 out of 3 in 2ahl

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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

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:
probe atom residue distance (Å) B Occ
A:Cu401

b:21.4
occ:1.00
NE2 A:HIS194 2.1 16.0 1.0
NE2 A:HIS190 2.1 12.0 1.0
NE2 A:HIS216 2.1 13.5 1.0
O B:HOH411 2.4 10.7 1.0
CE1 A:HIS216 3.0 9.9 1.0
CE1 A:HIS190 3.0 10.6 1.0
CE1 A:HIS194 3.0 14.6 1.0
CD2 A:HIS194 3.1 14.7 1.0
CD2 A:HIS190 3.1 10.9 1.0
CD2 A:HIS216 3.2 9.6 1.0
OH B:TYR98 4.0 16.1 1.0
CE2 B:TYR98 4.0 14.9 1.0
ND1 A:HIS216 4.1 10.1 1.0
ND1 A:HIS194 4.1 12.2 1.0
CE2 A:PHE212 4.1 12.5 1.0
ND1 A:HIS190 4.1 12.1 1.0
CU A:CU1400 4.2 28.6 1.0
CG A:HIS194 4.2 12.2 1.0
CG A:HIS190 4.2 11.4 1.0
CG A:HIS216 4.3 13.2 1.0
CZ B:TYR98 4.3 14.1 1.0
CD2 A:HIS215 4.4 14.4 1.0
NE2 A:HIS215 4.6 12.2 1.0
NE2 A:HIS63 4.6 13.3 1.0
CZ A:PHE212 4.8 10.9 1.0
CD2 A:PHE212 4.8 9.6 1.0
CE1 A:PHE59 4.9 8.8 1.0
CD2 B:TYR98 4.9 13.8 1.0
CD2 A:HIS63 5.0 10.4 1.0

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

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:
probe atom residue distance (Å) B Occ
B:Cu402

b:41.4
occ:1.00
NE2 B:HIS82 2.3 30.0 1.0
NE2 B:HIS97 2.3 31.0 1.0
SD B:MET84 2.5 33.3 1.0
O B:HOH746 2.7 35.8 1.0
CD2 B:HIS82 3.1 25.8 1.0
CE1 B:HIS97 3.3 26.6 1.0
CD2 B:HIS97 3.3 24.8 1.0
CE1 B:HIS82 3.4 27.5 1.0
CG B:MET84 3.4 24.3 1.0
CB B:MET84 3.5 16.2 1.0
O A:ILE42 3.5 15.2 1.0
CE B:MET84 3.7 24.6 1.0
CA A:MET43 4.0 15.7 1.0
O A:MET43 4.1 15.1 1.0
CG B:HIS82 4.3 23.4 1.0
C A:ILE42 4.4 17.5 1.0
ND1 B:HIS82 4.4 26.3 1.0
C A:MET43 4.4 14.9 1.0
ND1 B:HIS97 4.4 22.3 1.0
CG B:HIS97 4.5 23.4 1.0
N A:MET43 4.6 15.8 1.0
CA B:MET84 4.6 15.8 1.0
N B:MET84 4.7 14.3 1.0
O A:HOH720 4.7 18.2 1.0
CD1 B:ILE92 4.7 23.0 1.0
C B:VAL83 4.9 14.0 1.0
CB A:MET43 4.9 19.4 1.0
CG A:MET43 5.0 22.6 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: Thu Sep 3 16:29:06 2020
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