Atomistry » Copper » PDB 6ied-6l58 » 6jud
Atomistry »
  Copper »
    PDB 6ied-6l58 »
      6jud »

Copper in PDB 6jud: Radiation Damage in Aspergillus Oryzae Pro-Tyrosinase Oxygen-Bound C92A/H103F Mutant

Enzymatic activity of Radiation Damage in Aspergillus Oryzae Pro-Tyrosinase Oxygen-Bound C92A/H103F Mutant

All present enzymatic activity of Radiation Damage in Aspergillus Oryzae Pro-Tyrosinase Oxygen-Bound C92A/H103F Mutant:
1.14.18.1;

Protein crystallography data

The structure of Radiation Damage in Aspergillus Oryzae Pro-Tyrosinase Oxygen-Bound C92A/H103F Mutant, PDB code: 6jud was solved by N.Fujieda, K.Umakoshi, Y.Nishikawa, G.Kurisu, S.Itoh, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.00 / 1.56
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 54.413, 118.291, 79.547, 90.00, 91.01, 90.00
R / Rfree (%) 17.3 / 22.9

Copper Binding Sites:

The binding sites of Copper atom in the Radiation Damage in Aspergillus Oryzae Pro-Tyrosinase Oxygen-Bound C92A/H103F Mutant (pdb code 6jud). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 4 binding sites of Copper where determined in the Radiation Damage in Aspergillus Oryzae Pro-Tyrosinase Oxygen-Bound C92A/H103F Mutant, PDB code: 6jud:
Jump to Copper binding site number: 1; 2; 3; 4;

Copper binding site 1 out of 4 in 6jud

Go back to Copper Binding Sites List in 6jud
Copper binding site 1 out of 4 in the Radiation Damage in Aspergillus Oryzae Pro-Tyrosinase Oxygen-Bound C92A/H103F Mutant


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Radiation Damage in Aspergillus Oryzae Pro-Tyrosinase Oxygen-Bound C92A/H103F Mutant within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu701

b:25.9
occ:0.54
O A:HOH817 2.1 29.5 1.0
NE2 A:HIS94 2.1 25.5 1.0
NE2 A:HIS67 2.1 16.9 1.0
CE1 A:HIS67 3.0 16.4 1.0
CE1 A:HIS94 3.1 24.8 1.0
CD2 A:HIS94 3.1 27.4 1.0
CZ A:PHE103 3.2 14.4 1.0
CD2 A:HIS67 3.3 16.3 1.0
CE2 A:PHE513 3.5 14.7 1.0
CU A:CU702 3.7 13.9 0.7
CE1 A:PHE103 4.0 14.4 1.0
CE2 A:PHE103 4.0 15.5 1.0
CZ A:PHE513 4.1 13.1 1.0
ND1 A:HIS67 4.1 16.1 1.0
ND1 A:HIS94 4.2 25.9 1.0
CG A:HIS94 4.2 24.0 1.0
CG A:HIS67 4.3 14.8 1.0
NE2 A:HIS328 4.3 11.6 1.0
CE2 A:PHE368 4.4 12.2 1.0
NE2 A:HIS372 4.4 12.6 1.0
CE1 A:HIS328 4.5 13.5 1.0
CD2 A:PHE513 4.5 16.0 1.0
NE2 A:HIS332 4.6 13.7 1.0
CB A:ALA92 4.7 17.3 1.0
CZ A:PHE368 4.7 12.6 1.0
CE1 A:HIS372 4.9 10.9 1.0
CE1 A:HIS332 5.0 13.7 1.0

Copper binding site 2 out of 4 in 6jud

Go back to Copper Binding Sites List in 6jud
Copper binding site 2 out of 4 in the Radiation Damage in Aspergillus Oryzae Pro-Tyrosinase Oxygen-Bound C92A/H103F Mutant


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of Radiation Damage in Aspergillus Oryzae Pro-Tyrosinase Oxygen-Bound C92A/H103F Mutant within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu702

b:13.9
occ:0.73
O A:HOH817 1.7 29.5 1.0
NE2 A:HIS332 1.9 13.7 1.0
NE2 A:HIS372 2.0 12.6 1.0
NE2 A:HIS328 2.2 11.6 1.0
CE1 A:HIS332 2.9 13.7 1.0
CE1 A:HIS372 2.9 10.9 1.0
CD2 A:HIS328 2.9 12.4 1.0
CD2 A:HIS372 3.0 12.3 1.0
CD2 A:HIS332 3.0 11.3 1.0
CE1 A:HIS328 3.3 13.5 1.0
CU A:CU701 3.7 25.9 0.5
CE2 A:PHE368 3.8 12.2 1.0
ND1 A:HIS332 4.0 13.0 1.0
ND1 A:HIS372 4.0 11.8 1.0
CG A:HIS372 4.0 12.3 1.0
CG A:HIS332 4.1 11.3 1.0
CD2 A:HIS371 4.1 12.8 1.0
CG A:HIS328 4.2 12.3 1.0
ND1 A:HIS328 4.3 12.7 1.0
CD2 A:PHE368 4.3 10.1 1.0
CE2 A:PHE513 4.3 14.7 1.0
CZ A:PHE368 4.4 12.6 1.0
NE2 A:HIS371 4.5 11.4 1.0
CZ A:PHE513 4.6 13.1 1.0
CE1 A:PHE103 4.7 14.4 1.0
CZ A:PHE103 4.7 14.4 1.0

Copper binding site 3 out of 4 in 6jud

Go back to Copper Binding Sites List in 6jud
Copper binding site 3 out of 4 in the Radiation Damage in Aspergillus Oryzae Pro-Tyrosinase Oxygen-Bound C92A/H103F Mutant


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 3 of Radiation Damage in Aspergillus Oryzae Pro-Tyrosinase Oxygen-Bound C92A/H103F Mutant within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu701

b:18.7
occ:0.68
O1 B:PER703 1.8 23.4 0.9
O2 B:PER703 1.8 21.7 0.9
NE2 B:HIS94 1.9 22.7 1.0
NE2 B:HIS67 2.1 16.5 1.0
CE1 B:HIS94 2.7 21.2 1.0
CE1 B:HIS67 2.9 15.7 1.0
CD2 B:HIS94 3.1 23.3 1.0
CD2 B:HIS67 3.2 15.1 1.0
CZ B:PHE103 3.2 15.5 1.0
CU B:CU702 3.5 20.2 0.8
CE2 B:PHE513 3.5 17.0 1.0
ND1 B:HIS94 3.9 22.2 1.0
CE1 B:PHE103 4.0 13.7 1.0
ND1 B:HIS67 4.1 14.8 1.0
CE2 B:PHE103 4.1 15.0 1.0
CG B:HIS94 4.1 22.3 1.0
CZ B:PHE513 4.1 13.1 1.0
CG B:HIS67 4.3 13.3 1.0
NE2 B:HIS328 4.4 16.3 1.0
NE2 B:HIS372 4.5 16.8 1.0
CE2 B:PHE368 4.5 13.1 1.0
CE1 B:HIS328 4.6 18.3 1.0
CD2 B:PHE513 4.6 17.1 1.0
CB B:ALA92 4.6 17.1 1.0
NE2 B:HIS332 4.7 16.0 1.0
CZ B:PHE368 4.7 15.5 1.0
CG1 B:VAL359 4.9 31.6 1.0
CE1 B:HIS372 5.0 13.5 1.0

Copper binding site 4 out of 4 in 6jud

Go back to Copper Binding Sites List in 6jud
Copper binding site 4 out of 4 in the Radiation Damage in Aspergillus Oryzae Pro-Tyrosinase Oxygen-Bound C92A/H103F Mutant


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 4 of Radiation Damage in Aspergillus Oryzae Pro-Tyrosinase Oxygen-Bound C92A/H103F Mutant within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu702

b:20.2
occ:0.84
O2 B:PER703 1.9 21.7 0.9
NE2 B:HIS332 2.0 16.0 1.0
NE2 B:HIS328 2.0 16.3 1.0
NE2 B:HIS372 2.0 16.8 1.0
O1 B:PER703 2.2 23.4 0.9
CD2 B:HIS328 2.9 14.6 1.0
CE1 B:HIS332 2.9 12.7 1.0
CE1 B:HIS372 2.9 13.5 1.0
CD2 B:HIS332 3.0 14.7 1.0
CE1 B:HIS328 3.1 18.3 1.0
CD2 B:HIS372 3.1 15.5 1.0
CU B:CU701 3.5 18.7 0.7
CE2 B:PHE368 3.9 13.1 1.0
ND1 B:HIS332 4.0 13.2 1.0
CG B:HIS328 4.0 14.5 1.0
ND1 B:HIS372 4.1 14.7 1.0
ND1 B:HIS328 4.1 15.5 1.0
CG B:HIS332 4.1 12.1 1.0
CE2 B:PHE513 4.1 17.0 1.0
CG B:HIS372 4.2 14.0 1.0
CD2 B:HIS371 4.4 13.1 1.0
CZ B:PHE513 4.5 13.1 1.0
CZ B:PHE103 4.5 15.5 1.0
CE1 B:PHE103 4.6 13.7 1.0
CZ B:PHE368 4.6 15.5 1.0
CD2 B:PHE368 4.6 11.5 1.0
NE2 B:HIS371 4.7 12.6 1.0
NE2 B:HIS67 4.9 16.5 1.0
NE2 B:HIS94 4.9 22.7 1.0

Reference:

N.Fujieda, K.Umakoshi, Y.Ochi, Y.Nishikawa, S.Yanagisawa, M.Kubo, G.Kurisu, S.Itoh. Copper-Oxygen Dynamics in Tyrosinase Mechanism. Angew.Chem.Int.Ed.Engl. 2020.
ISSN: ESSN 1521-3773
PubMed: 32356371
DOI: 10.1002/ANIE.202004733
Page generated: Mon Jul 14 06:22:21 2025

Last articles

Fe in 2YXO
Fe in 2YRS
Fe in 2YXC
Fe in 2YNM
Fe in 2YVJ
Fe in 2YP1
Fe in 2YU2
Fe in 2YU1
Fe in 2YQB
Fe in 2YOO
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy