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Copper in PDB 1hfu: Type-2 Cu-Depleted Laccase From Coprinus Cinereus at 1.68 A Resolution

Enzymatic activity of Type-2 Cu-Depleted Laccase From Coprinus Cinereus at 1.68 A Resolution

All present enzymatic activity of Type-2 Cu-Depleted Laccase From Coprinus Cinereus at 1.68 A Resolution:
1.10.3.2;

Protein crystallography data

The structure of Type-2 Cu-Depleted Laccase From Coprinus Cinereus at 1.68 A Resolution, PDB code: 1hfu was solved by V.Ducros, A.M.Brzozowski, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 15.00 / 1.68
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 45.120, 84.560, 139.030, 90.00, 90.00, 90.00
R / Rfree (%) 18.4 / 20.8

Copper Binding Sites:

The binding sites of Copper atom in the Type-2 Cu-Depleted Laccase From Coprinus Cinereus at 1.68 A Resolution (pdb code 1hfu). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 3 binding sites of Copper where determined in the Type-2 Cu-Depleted Laccase From Coprinus Cinereus at 1.68 A Resolution, PDB code: 1hfu:
Jump to Copper binding site number: 1; 2; 3;

Copper binding site 1 out of 3 in 1hfu

Go back to Copper Binding Sites List in 1hfu
Copper binding site 1 out of 3 in the Type-2 Cu-Depleted Laccase From Coprinus Cinereus at 1.68 A Resolution


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Type-2 Cu-Depleted Laccase From Coprinus Cinereus at 1.68 A Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu701

b:20.9
occ:1.00
ND1 A:HIS457 2.0 18.4 1.0
ND1 A:HIS396 2.1 16.7 1.0
SG A:CYS452 2.2 15.2 1.0
CE1 A:HIS457 2.9 18.7 1.0
CE1 A:HIS396 3.0 17.2 1.0
CG A:HIS457 3.1 17.3 1.0
CG A:HIS396 3.2 17.1 1.0
CB A:CYS452 3.2 14.0 1.0
CB A:HIS457 3.4 17.3 1.0
CB A:HIS396 3.5 16.8 1.0
CD2 A:LEU462 3.5 17.5 1.0
CD1 A:ILE454 3.8 20.0 1.0
CA A:HIS396 3.9 15.4 1.0
CB A:ILE454 3.9 16.1 1.0
NE2 A:HIS457 4.1 19.3 1.0
NE2 A:HIS396 4.1 18.4 1.0
CG1 A:ILE454 4.1 17.4 1.0
CD2 A:HIS457 4.2 17.3 1.0
CD2 A:HIS396 4.3 18.5 1.0
CA A:CYS452 4.6 13.7 1.0
CD A:PRO397 4.6 14.9 1.0
CG2 A:ILE454 4.6 16.5 1.0
O A:GLY393 4.8 19.1 1.0
N A:ILE454 4.8 14.8 1.0
C A:HIS396 4.8 17.5 1.0
N A:HIS396 4.9 17.4 1.0
CG A:LEU462 4.9 17.1 1.0
CA A:ILE454 4.9 18.2 1.0
CA A:HIS457 4.9 21.5 1.0
N A:PRO397 5.0 15.4 1.0

Copper binding site 2 out of 3 in 1hfu

Go back to Copper Binding Sites List in 1hfu
Copper binding site 2 out of 3 in the Type-2 Cu-Depleted Laccase From Coprinus Cinereus at 1.68 A Resolution


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of Type-2 Cu-Depleted Laccase From Coprinus Cinereus at 1.68 A Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu702

b:23.3
occ:1.00
NE2 A:HIS451 2.0 18.8 1.0
NE2 A:HIS111 2.0 20.1 1.0
NE2 A:HIS401 2.0 13.6 1.0
O A:HOH2386 2.2 24.8 1.0
NE2 A:HIS399 2.5 18.8 0.3
CE1 A:HIS401 2.8 13.8 1.0
CE1 A:HIS111 2.8 20.8 1.0
CE1 A:HIS451 2.9 16.6 1.0
CD2 A:HIS451 3.1 20.4 1.0
CD2 A:HIS111 3.1 20.2 1.0
CD2 A:HIS401 3.2 15.7 1.0
CD2 A:HIS399 3.3 21.1 0.3
CE1 A:HIS399 3.6 18.6 0.3
CD2 A:HIS399 3.9 14.6 0.7
ND1 A:HIS401 4.0 14.9 1.0
ND1 A:HIS111 4.0 20.7 1.0
ND1 A:HIS451 4.1 16.2 1.0
CD2 A:PHE449 4.2 16.9 1.0
O A:HOH2423 4.2 37.8 1.0
CG A:HIS451 4.2 16.3 1.0
CG A:HIS111 4.2 19.4 1.0
CG A:HIS401 4.2 10.6 1.0
CB A:PHE449 4.3 13.2 1.0
CG A:HIS399 4.5 20.4 0.3
CD2 A:HIS64 4.5 16.9 1.0
CG A:PHE449 4.6 12.5 1.0
ND1 A:HIS399 4.6 21.9 0.3
NE2 A:HIS64 4.7 16.9 1.0
NE2 A:HIS399 4.8 13.7 0.7
CG A:HIS399 5.0 15.3 0.7

Copper binding site 3 out of 3 in 1hfu

Go back to Copper Binding Sites List in 1hfu
Copper binding site 3 out of 3 in the Type-2 Cu-Depleted Laccase From Coprinus Cinereus at 1.68 A Resolution


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 3 of Type-2 Cu-Depleted Laccase From Coprinus Cinereus at 1.68 A Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu703

b:19.6
occ:1.00
ND1 A:HIS66 2.0 14.5 1.0
NE2 A:HIS109 2.0 16.0 1.0
NE2 A:HIS453 2.1 17.0 1.0
CE1 A:HIS66 2.8 17.0 1.0
CD2 A:HIS109 3.0 15.2 1.0
CE1 A:HIS109 3.0 17.2 1.0
CE1 A:HIS453 3.0 13.7 1.0
CG A:HIS66 3.0 15.3 1.0
CD2 A:HIS453 3.2 15.5 1.0
O A:HOH2386 3.3 24.8 1.0
CZ2 A:TRP107 3.4 13.2 1.0
CB A:HIS66 3.4 13.1 1.0
CD2 A:HIS64 3.7 16.9 1.0
CE2 A:TRP107 3.7 11.5 1.0
NE1 A:TRP107 3.9 13.7 1.0
CE1 A:HIS399 4.0 18.6 0.3
NE2 A:HIS66 4.0 13.4 1.0
ND1 A:HIS109 4.1 16.1 1.0
CG A:HIS109 4.1 13.6 1.0
CH2 A:TRP107 4.1 13.0 1.0
CD2 A:HIS66 4.1 16.3 1.0
ND1 A:HIS453 4.2 14.6 1.0
NE2 A:HIS64 4.2 16.9 1.0
CD2 A:HIS399 4.3 14.6 0.7
NE2 A:HIS399 4.3 18.8 0.3
CG A:HIS453 4.3 14.1 1.0
NE2 A:HIS399 4.4 13.7 0.7
ND1 A:HIS399 4.4 21.9 0.3
CA A:HIS66 4.6 11.2 1.0
CD2 A:TRP107 4.7 12.9 1.0
CG A:HIS64 4.9 17.1 1.0
CD2 A:HIS399 4.9 21.1 0.3
CG A:HIS399 4.9 20.4 0.3
CD1 A:TRP107 5.0 13.0 1.0
CZ3 A:TRP107 5.0 11.5 1.0

Reference:

V.Ducros, A.M.Brzozowski, K.S.Wilson, P.Ostergaard, P.Schneider, A.Svendson, G.J.Davies. Structure of the Laccase From Coprinus Cinereus at 1.68A Resolution: Evidence For Different Type 2 Cu-Depleted Isoforms Acta Crystallogr.,Sect.D V. 57 333 2001.
ISSN: ISSN 0907-4449
PubMed: 11173497
DOI: 10.1107/S0907444900013779
Page generated: Sun Dec 13 10:59:13 2020

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