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Copper in PDB 2wsd: Proximal Mutations at the Type 1 Cu Site of Cota-Laccase: I494A Mutant

Enzymatic activity of Proximal Mutations at the Type 1 Cu Site of Cota-Laccase: I494A Mutant

All present enzymatic activity of Proximal Mutations at the Type 1 Cu Site of Cota-Laccase: I494A Mutant:
1.10.3.2;

Protein crystallography data

The structure of Proximal Mutations at the Type 1 Cu Site of Cota-Laccase: I494A Mutant, PDB code: 2wsd was solved by C.S.Silva, P.Durao, Z.Chen, C.M.Soares, M.M.Pereira, S.Todorovic, P.Hildebrandt, L.O.Martins, P.F.Lindley, I.Bento, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 29.99 / 1.60
Space group P 31 2 1
Cell size a, b, c (Å), α, β, γ (°) 101.868, 101.868, 137.037, 90.00, 90.00, 120.00
R / Rfree (%) 17.7 / 19

Copper Binding Sites:

The binding sites of Copper atom in the Proximal Mutations at the Type 1 Cu Site of Cota-Laccase: I494A Mutant (pdb code 2wsd). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 4 binding sites of Copper where determined in the Proximal Mutations at the Type 1 Cu Site of Cota-Laccase: I494A Mutant, PDB code: 2wsd:
Jump to Copper binding site number: 1; 2; 3; 4;

Copper binding site 1 out of 4 in 2wsd

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Copper binding site 1 out of 4 in the Proximal Mutations at the Type 1 Cu Site of Cota-Laccase: I494A Mutant


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Proximal Mutations at the Type 1 Cu Site of Cota-Laccase: I494A Mutant within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu601

b:21.3
occ:1.00
ND1 A:HIS497 2.0 18.9 1.0
ND1 A:HIS419 2.0 20.1 1.0
SG A:CYS492 2.3 17.4 1.0
CE1 A:HIS419 2.9 20.2 1.0
CE1 A:HIS497 3.0 19.4 1.0
CG A:HIS497 3.0 17.8 1.0
O A:HOH2519 3.0 28.5 1.0
CG A:HIS419 3.1 18.8 1.0
CB A:CYS492 3.3 16.0 1.0
SD A:MET502 3.3 19.4 1.0
CB A:HIS497 3.3 17.6 1.0
CB A:HIS419 3.6 18.2 1.0
NE2 A:HIS419 4.1 20.2 1.0
CB A:ALA494 4.1 15.3 1.0
CE A:MET502 4.1 22.1 1.0
NE2 A:HIS497 4.1 19.4 1.0
CA A:HIS419 4.1 18.0 1.0
CD2 A:HIS497 4.1 18.0 1.0
CD2 A:HIS419 4.2 20.2 1.0
CD2 A:LEU386 4.5 24.0 0.5
CD A:PRO420 4.6 16.3 1.0
CA A:CYS492 4.6 15.8 1.0
O A:THR418 4.7 20.5 1.0
CG A:MET502 4.8 18.4 1.0
CA A:HIS497 4.9 17.4 1.0
O A:HOH2518 4.9 34.1 1.0
N A:ALA494 5.0 15.4 1.0

Copper binding site 2 out of 4 in 2wsd

Go back to Copper Binding Sites List in 2wsd
Copper binding site 2 out of 4 in the Proximal Mutations at the Type 1 Cu Site of Cota-Laccase: I494A Mutant


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of Proximal Mutations at the Type 1 Cu Site of Cota-Laccase: I494A Mutant within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu602

b:15.4
occ:1.00
NE2 A:HIS153 2.0 16.3 1.0
ND1 A:HIS107 2.0 14.8 1.0
NE2 A:HIS493 2.0 16.6 1.0
O1 A:OXY605 2.6 7.7 1.0
O2 A:OXY605 2.7 23.2 1.0
CE1 A:HIS107 2.9 15.2 1.0
CE1 A:HIS153 3.0 15.2 1.0
CD2 A:HIS153 3.0 13.2 1.0
CE1 A:HIS493 3.0 14.8 1.0
CD2 A:HIS493 3.1 15.9 1.0
CG A:HIS107 3.1 13.7 1.0
CB A:HIS107 3.4 13.2 1.0
CZ2 A:TRP151 3.8 13.4 1.0
CU A:CU604 4.0 19.0 1.0
CD2 A:HIS105 4.1 15.0 1.0
ND1 A:HIS153 4.1 13.9 1.0
NE2 A:HIS107 4.1 14.3 1.0
CE2 A:TRP151 4.1 12.5 1.0
ND1 A:HIS493 4.1 15.3 1.0
CG A:HIS153 4.1 12.9 1.0
CD2 A:HIS107 4.2 15.4 1.0
CG A:HIS493 4.2 15.1 1.0
NE1 A:TRP151 4.2 13.5 1.0
CB A:ALA297 4.4 14.3 1.0
CH2 A:TRP151 4.5 12.9 1.0
NE2 A:HIS105 4.6 16.1 1.0
CD2 A:HIS422 4.6 15.9 1.0
NE2 A:HIS422 4.6 15.7 1.0
CA A:HIS107 4.6 13.6 1.0
CU A:CU603 4.8 16.9 1.0

Copper binding site 3 out of 4 in 2wsd

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Copper binding site 3 out of 4 in the Proximal Mutations at the Type 1 Cu Site of Cota-Laccase: I494A Mutant


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 3 of Proximal Mutations at the Type 1 Cu Site of Cota-Laccase: I494A Mutant within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu603

b:16.9
occ:1.00
NE2 A:HIS491 2.0 15.5 1.0
NE2 A:HIS424 2.0 17.1 1.0
NE2 A:HIS155 2.0 16.4 1.0
O2 A:OXY605 2.3 23.2 1.0
O1 A:OXY605 2.3 7.7 1.0
CE1 A:HIS424 2.9 18.0 1.0
CE1 A:HIS491 2.9 16.3 1.0
CD2 A:HIS155 3.0 15.8 1.0
CD2 A:HIS491 3.0 15.1 1.0
CE1 A:HIS155 3.1 16.8 1.0
CD2 A:HIS424 3.1 17.8 1.0
CU A:CU604 3.6 19.0 1.0
CD2 A:HIS422 3.8 15.9 1.0
CD2 A:HIS105 4.0 15.0 1.0
ND1 A:HIS491 4.0 15.9 1.0
CG2 A:VAL489 4.1 15.0 0.5
ND1 A:HIS424 4.1 16.2 1.0
NE2 A:HIS105 4.1 16.1 1.0
CG A:HIS491 4.1 14.8 1.0
CG A:HIS155 4.2 15.2 1.0
ND1 A:HIS155 4.2 17.1 1.0
CG A:HIS424 4.2 15.7 1.0
NE2 A:HIS422 4.2 15.7 1.0
OE2 A:GLU498 4.5 19.7 1.0
O A:HOH2199 4.6 25.4 1.0
CG A:HIS105 4.7 13.5 1.0
CE1 A:HIS105 4.8 17.2 1.0
CU A:CU602 4.8 15.4 1.0
CD2 A:HIS493 5.0 15.9 1.0
CG1 A:VAL489 5.0 15.5 0.5

Copper binding site 4 out of 4 in 2wsd

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Copper binding site 4 out of 4 in the Proximal Mutations at the Type 1 Cu Site of Cota-Laccase: I494A Mutant


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 4 of Proximal Mutations at the Type 1 Cu Site of Cota-Laccase: I494A Mutant within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu604

b:19.0
occ:1.00
NE2 A:HIS422 2.0 15.7 1.0
NE2 A:HIS105 2.0 16.1 1.0
O1 A:OXY605 2.6 7.7 1.0
CD2 A:HIS422 2.9 15.9 1.0
CD2 A:HIS105 2.9 15.0 1.0
CE1 A:HIS105 3.0 17.2 1.0
CE1 A:HIS422 3.0 16.9 1.0
O A:HOH2177 3.0 17.5 1.0
NE2 A:HIS424 3.2 17.1 1.0
CD2 A:HIS424 3.3 17.8 1.0
O2 A:OXY605 3.4 23.2 1.0
ND1 A:HIS107 3.5 14.8 1.0
CU A:CU603 3.6 16.9 1.0
CG A:HIS107 3.7 13.7 1.0
CE1 A:HIS424 3.8 18.0 1.0
CG A:HIS424 3.8 15.7 1.0
CA A:HIS107 3.9 13.6 1.0
CE1 A:HIS107 3.9 15.2 1.0
CG A:HIS105 4.0 13.5 1.0
ND1 A:HIS105 4.0 15.5 1.0
CU A:CU602 4.0 15.4 1.0
CG A:HIS422 4.0 14.8 1.0
ND1 A:HIS422 4.1 15.3 1.0
ND1 A:HIS424 4.1 16.2 1.0
CB A:HIS107 4.1 13.2 1.0
CD2 A:HIS107 4.2 15.4 1.0
NE2 A:HIS107 4.3 14.3 1.0
N A:GLY108 4.4 14.4 1.0
CA A:HIS424 4.6 16.4 1.0
CB A:HIS424 4.7 16.3 1.0
C A:HIS107 4.7 14.2 1.0
NE2 A:HIS491 4.8 15.5 1.0
N A:HIS107 4.8 13.3 1.0
O A:LEU106 5.0 13.5 1.0
O A:HOH2196 5.0 17.9 1.0

Reference:

P.Durao, Z.Chen, C.S.Silva, C.M.Soares, M.M.Pereira, S.Todorovic, P.Hildebrandt, I.Bento, P.F.Lindley, L.O.Martins. Proximal Mutations at the Type 1 Copper Site of Cota Laccase: Spectroscopic, Redox, Kinetic and Structural Characterization of I494A and L386A Mutants. Biochem.J. V. 412 339 2008.
ISSN: ISSN 0264-6021
PubMed: 18307408
DOI: 10.1042/BJ20080166
Page generated: Thu Sep 3 16:53:03 2020
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