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Copper in PDB 2hrh: Crystal Structure of Blue Laccase From Trametes Trogii

Enzymatic activity of Crystal Structure of Blue Laccase From Trametes Trogii

All present enzymatic activity of Crystal Structure of Blue Laccase From Trametes Trogii:
1.10.3.2;

Protein crystallography data

The structure of Crystal Structure of Blue Laccase From Trametes Trogii, PDB code: 2hrh was solved by I.Matera, A.Gullotto, M.Ferraroni, S.Tilli, F.Briganti, A.Scozzafava, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 39.53 / 2.60
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 84.932, 84.327, 108.383, 90.00, 90.00, 90.00
R / Rfree (%) 17.5 / 23.3

Copper Binding Sites:

The binding sites of Copper atom in the Crystal Structure of Blue Laccase From Trametes Trogii (pdb code 2hrh). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 4 binding sites of Copper where determined in the Crystal Structure of Blue Laccase From Trametes Trogii, PDB code: 2hrh:
Jump to Copper binding site number: 1; 2; 3; 4;

Copper binding site 1 out of 4 in 2hrh

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Copper binding site 1 out of 4 in the Crystal Structure of Blue Laccase From Trametes Trogii


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 Blue Laccase From Trametes Trogii within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu497

b:39.4
occ:1.00
ND1 A:HIS455 2.1 30.9 1.0
ND1 A:HIS394 2.1 28.5 1.0
SG A:CYS450 2.1 28.1 1.0
CE1 A:HIS394 3.0 29.6 1.0
CG A:HIS455 3.0 29.9 1.0
CE1 A:HIS455 3.1 28.8 1.0
CG A:HIS394 3.1 25.4 1.0
CB A:HIS455 3.3 30.0 1.0
CB A:CYS450 3.5 25.2 1.0
CB A:HIS394 3.5 24.7 1.0
CD1 A:ILE452 3.6 27.8 1.0
CB A:ILE452 3.6 28.2 1.0
CD2 A:PHE460 3.7 24.9 1.0
CG1 A:ILE452 3.8 26.7 1.0
CE2 A:PHE460 3.9 25.0 1.0
CA A:HIS394 4.0 24.9 1.0
NE2 A:HIS394 4.1 28.4 1.0
NE2 A:HIS455 4.2 29.2 1.0
CD2 A:HIS455 4.2 28.1 1.0
CD2 A:HIS394 4.2 27.8 1.0
CG2 A:ILE452 4.4 28.2 1.0
O A:GLY391 4.4 31.4 1.0
N A:ILE452 4.7 28.1 1.0
CA A:ILE452 4.7 28.4 1.0
CA A:CYS450 4.8 26.1 1.0
CD A:PRO395 4.8 23.6 1.0
CA A:HIS455 4.9 30.8 1.0
O A:ILE452 4.9 28.3 1.0
C A:HIS394 4.9 24.6 1.0
N A:HIS394 5.0 25.1 1.0

Copper binding site 2 out of 4 in 2hrh

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Copper binding site 2 out of 4 in the Crystal Structure of Blue Laccase From Trametes Trogii


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 Blue Laccase From Trametes Trogii within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu498

b:59.5
occ:1.00
NE2 A:HIS397 1.8 31.0 1.0
NE2 A:HIS64 2.1 29.8 1.0
CE1 A:HIS397 2.8 28.8 1.0
CD2 A:HIS397 2.8 28.4 1.0
CD2 A:HIS64 3.0 25.0 1.0
CE1 A:HIS64 3.0 27.9 1.0
NE2 A:HIS399 3.3 28.0 1.0
CU A:CU500 3.3 44.3 1.0
ND1 A:HIS66 3.4 21.4 1.0
CE1 A:HIS399 3.5 24.1 1.0
CU A:CU499 3.6 38.0 1.0
CG A:HIS66 3.6 23.4 1.0
CD2 A:HIS399 3.6 25.6 1.0
CE1 A:HIS66 3.7 23.5 1.0
CA A:HIS66 3.8 24.1 1.0
ND1 A:HIS399 3.8 25.0 1.0
ND1 A:HIS397 3.9 30.0 1.0
CG A:HIS397 3.9 26.8 1.0
CG A:HIS399 3.9 26.5 1.0
CD2 A:HIS66 4.0 21.1 1.0
NE2 A:HIS66 4.0 21.1 1.0
ND1 A:HIS64 4.1 27.3 1.0
CB A:HIS66 4.1 24.1 1.0
CG A:HIS64 4.1 25.9 1.0
N A:GLY67 4.2 25.4 1.0
C A:HIS66 4.5 25.0 1.0
O A:HOH1106 4.6 42.5 1.0
CA A:HIS399 4.7 27.1 1.0
N A:HIS66 4.8 24.7 1.0
O A:HOH1017 4.8 26.2 1.0
CB A:HIS399 4.9 27.2 1.0
NE2 A:HIS109 4.9 20.8 1.0

Copper binding site 3 out of 4 in 2hrh

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Copper binding site 3 out of 4 in the Crystal Structure of Blue Laccase From Trametes Trogii


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 Blue Laccase From Trametes Trogii within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu499

b:38.0
occ:1.00
NE2 A:HIS399 2.1 28.0 1.0
NE2 A:HIS449 2.2 31.3 1.0
NE2 A:HIS111 2.4 21.0 1.0
CE1 A:HIS399 3.0 24.1 1.0
CE1 A:HIS449 3.1 30.7 1.0
CD2 A:HIS111 3.2 19.9 1.0
CU A:CU500 3.2 44.3 1.0
CD2 A:HIS397 3.2 28.4 1.0
CD2 A:HIS399 3.2 25.6 1.0
CD2 A:HIS449 3.2 29.6 1.0
CE1 A:HIS111 3.5 22.1 1.0
CU A:CU498 3.6 59.5 1.0
NE2 A:HIS397 3.8 31.0 1.0
CD2 A:HIS64 4.1 25.0 1.0
ND1 A:HIS399 4.1 25.0 1.0
NE2 A:HIS64 4.2 29.8 1.0
ND1 A:HIS449 4.3 28.8 1.0
CG A:HIS399 4.3 26.5 1.0
CG A:HIS449 4.4 28.1 1.0
CE1 A:HIS109 4.4 21.1 1.0
CG A:HIS397 4.4 26.8 1.0
CG A:HIS111 4.4 22.6 1.0
NE2 A:HIS451 4.4 28.5 1.0
CD2 A:HIS451 4.5 25.0 1.0
ND1 A:HIS111 4.6 23.1 1.0
NE2 A:HIS109 4.8 20.8 1.0
CG A:HIS64 4.8 25.9 1.0
ND1 A:HIS66 5.0 21.4 1.0

Copper binding site 4 out of 4 in 2hrh

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Copper binding site 4 out of 4 in the Crystal Structure of Blue Laccase From Trametes Trogii


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 4 of Crystal Structure of Blue Laccase From Trametes Trogii within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu500

b:44.3
occ:1.00
ND1 A:HIS66 2.1 21.4 1.0
NE2 A:HIS109 2.3 20.8 1.0
NE2 A:HIS451 2.4 28.5 1.0
CE1 A:HIS66 2.7 23.5 1.0
CE1 A:HIS109 2.9 21.1 1.0
CD2 A:HIS451 3.1 25.0 1.0
CU A:CU499 3.2 38.0 1.0
CU A:CU498 3.3 59.5 1.0
CG A:HIS66 3.3 23.4 1.0
CE1 A:HIS451 3.5 26.5 1.0
CD2 A:HIS64 3.6 25.0 1.0
CD2 A:HIS109 3.6 21.2 1.0
CD2 A:HIS397 3.7 28.4 1.0
NE2 A:HIS397 3.8 31.0 1.0
NE2 A:HIS66 3.9 21.1 1.0
CB A:HIS66 4.0 24.1 1.0
NE2 A:HIS64 4.0 29.8 1.0
ND1 A:HIS109 4.1 18.9 1.0
CD2 A:HIS66 4.2 21.1 1.0
CG A:HIS451 4.3 25.2 1.0
ND1 A:HIS451 4.5 25.9 1.0
CG A:HIS109 4.5 21.1 1.0
CZ2 A:TRP107 4.5 20.3 1.0
CG A:HIS397 4.6 26.8 1.0
NE2 A:HIS449 4.6 31.3 1.0
CD2 A:HIS111 4.7 19.9 1.0
CE1 A:HIS397 4.7 28.8 1.0
NE2 A:HIS399 4.7 28.0 1.0
CA A:HIS66 4.8 24.1 1.0
NE2 A:HIS111 4.8 21.0 1.0
CE1 A:HIS449 4.8 30.7 1.0
CG A:HIS64 4.8 25.9 1.0
CB A:ALA240 4.9 23.1 1.0
CE2 A:TRP107 4.9 19.6 1.0
NE1 A:TRP107 4.9 21.5 1.0

Reference:

I.Matera, A.Gullotto, S.Tilli, M.Ferraroni, A.Scozzafava, F.Briganti. Crystal Structure of the Blue Multicopper Oxidase From the White-Rot Fungus Trametes Trogii Complexed with P-Toluate Inorg.Chim.Acta. V. 361 4129 2008.
ISSN: ISSN 0020-1693
DOI: 10.1016/J.ICA.2008.03.091
Page generated: Wed Oct 28 14:19:54 2020
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