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Copper in PDB 2hrg: Crystal Structure of Blue Laccase From Trametes Trogii Complexed with P-Methylbenzoate

Enzymatic activity of Crystal Structure of Blue Laccase From Trametes Trogii Complexed with P-Methylbenzoate

All present enzymatic activity of Crystal Structure of Blue Laccase From Trametes Trogii Complexed with P-Methylbenzoate:
1.10.3.2;

Protein crystallography data

The structure of Crystal Structure of Blue Laccase From Trametes Trogii Complexed with P-Methylbenzoate, PDB code: 2hrg 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) 22.33 / 1.58
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 84.385, 85.128, 108.561, 90.00, 90.00, 90.00
R / Rfree (%) 17.4 / 19.2

Other elements in 2hrg:

The structure of Crystal Structure of Blue Laccase From Trametes Trogii Complexed with P-Methylbenzoate also contains other interesting chemical elements:

Calcium (Ca) 3 atoms

Copper Binding Sites:

The binding sites of Copper atom in the Crystal Structure of Blue Laccase From Trametes Trogii Complexed with P-Methylbenzoate (pdb code 2hrg). 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 Complexed with P-Methylbenzoate, PDB code: 2hrg:
Jump to Copper binding site number: 1; 2; 3; 4;

Copper binding site 1 out of 4 in 2hrg

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Copper binding site 1 out of 4 in the Crystal Structure of Blue Laccase From Trametes Trogii Complexed with P-Methylbenzoate


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 Complexed with P-Methylbenzoate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu1497

b:14.1
occ:1.00
 ND1 A:HIS455 2.0 13.3 1.0
ND1 A:HIS394 2.1 12.7 1.0
SG A:CYS450 2.1 12.1 1.0
CE1 A:HIS394 3.0 14.3 1.0
CE1 A:HIS455 3.0 14.4 1.0
CG A:HIS455 3.0 12.6 1.0
CG A:HIS394 3.1 11.6 1.0
CB A:CYS450 3.2 11.2 1.0
CB A:HIS455 3.4 13.9 1.0
CB A:HIS394 3.4 12.2 1.0
CD1 A:ILE452 3.6 12.4 1.0
CB A:ILE452 3.7 12.2 1.0
CD2 A:PHE460 3.8 11.1 1.0
CA A:HIS394 4.0 12.2 1.0
CG1 A:ILE452 4.0 12.3 1.0
CE2 A:PHE460 4.0 12.0 1.0
NE2 A:HIS394 4.1 14.0 1.0
NE2 A:HIS455 4.1 13.9 1.0
CD2 A:HIS394 4.2 13.1 1.0
CD2 A:HIS455 4.2 14.2 1.0
CG2 A:ILE452 4.6 12.3 1.0
CA A:CYS450 4.6 10.8 1.0
CD A:PRO395 4.6 11.9 1.0
N A:ILE452 4.7 11.9 1.0
O A:GLY391 4.7 15.0 1.0
CA A:ILE452 4.8 12.4 1.0
O A:ILE452 4.9 13.1 1.0
CA A:HIS455 4.9 13.7 1.0
N A:HIS394 4.9 12.4 1.0
C A:HIS394 4.9 11.7 1.0

Copper binding site 2 out of 4 in 2hrg

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Copper binding site 2 out of 4 in the Crystal Structure of Blue Laccase From Trametes Trogii Complexed with P-Methylbenzoate


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 Complexed with P-Methylbenzoate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu1498

b:13.4
occ:1.00
 ND1 A:HIS66 1.9 10.5 1.0
NE2 A:HIS109 2.0 12.1 1.0
NE2 A:HIS451 2.2 10.7 1.0
CE1 A:HIS66 2.9 10.0 1.0
O A:HOH3160 3.0 22.0 1.0
CE1 A:HIS109 3.0 11.9 1.0
CG A:HIS66 3.0 9.6 1.0
CD2 A:HIS109 3.0 11.2 1.0
CE1 A:HIS451 3.1 10.4 1.0
CD2 A:HIS451 3.2 10.6 1.0
CB A:HIS66 3.4 10.0 1.0
CZ2 A:TRP107 3.6 8.7 1.0
CD2 A:HIS64 3.7 10.5 1.0
CE2 A:TRP107 3.9 8.2 1.0
NE1 A:TRP107 4.0 9.8 1.0
NE2 A:HIS66 4.0 11.4 1.0
CU A:CU1499 4.1 22.6 1.0
CD2 A:HIS66 4.1 10.9 1.0
ND1 A:HIS109 4.1 10.6 1.0
CG A:HIS109 4.1 9.4 1.0
NE2 A:HIS64 4.2 11.3 1.0
ND1 A:HIS451 4.2 10.4 1.0
CB A:ALA240 4.3 9.5 1.0
CH2 A:TRP107 4.3 8.8 1.0
CG A:HIS451 4.3 10.2 1.0
CD2 A:HIS397 4.3 11.3 1.0
O A:HOH3077 4.4 19.9 1.0
NE2 A:HIS397 4.5 11.5 1.0
CA A:HIS66 4.6 9.8 1.0
CD2 A:TRP107 4.8 8.9 1.0
CG A:HIS64 4.9 10.4 1.0
CD1 A:TRP107 5.0 9.1 1.0

Copper binding site 3 out of 4 in 2hrg

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Copper binding site 3 out of 4 in the Crystal Structure of Blue Laccase From Trametes Trogii Complexed with P-Methylbenzoate


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 Complexed with P-Methylbenzoate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu1499

b:22.6
occ:1.00
 NE2 A:HIS397 1.8 11.5 1.0
NE2 A:HIS64 1.9 11.3 1.0
O A:HOH3036 2.6 14.0 1.0
CE1 A:HIS64 2.8 12.0 1.0
CD2 A:HIS397 2.8 11.3 1.0
CE1 A:HIS397 2.8 12.5 1.0
CD2 A:HIS64 2.9 10.5 1.0
NE2 A:HIS399 3.4 11.3 1.0
ND1 A:HIS66 3.4 10.5 1.0
CE1 A:HIS399 3.4 11.8 1.0
ND1 A:HIS399 3.6 10.2 1.0
CG A:HIS66 3.7 9.6 1.0
CD2 A:HIS399 3.7 10.4 1.0
O A:HOH3160 3.7 22.0 1.0
CE1 A:HIS66 3.8 10.0 1.0
CG A:HIS399 3.8 10.0 1.0
ND1 A:HIS64 3.9 9.9 1.0
CA A:HIS66 3.9 9.8 1.0
ND1 A:HIS397 3.9 12.9 1.0
CG A:HIS397 3.9 11.1 1.0
CG A:HIS64 4.0 10.4 1.0
CD2 A:HIS66 4.1 10.9 1.0
CU A:CU1498 4.1 13.4 1.0
CB A:HIS66 4.1 10.0 1.0
NE2 A:HIS66 4.1 11.4 1.0
N A:GLY67 4.1 11.0 1.0
C A:HIS66 4.5 10.7 1.0
CU A:CU1500 4.5 14.7 1.0
O A:HOH3011 4.6 11.8 1.0
CA A:HIS399 4.6 10.9 1.0
CB A:HIS399 4.7 11.2 1.0
O A:HOH3017 4.7 14.3 1.0
N A:HIS66 4.9 9.5 1.0

Copper binding site 4 out of 4 in 2hrg

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Copper binding site 4 out of 4 in the Crystal Structure of Blue Laccase From Trametes Trogii Complexed with P-Methylbenzoate


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 Complexed with P-Methylbenzoate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu1500

b:14.7
occ:1.00
 NE2 A:HIS449 2.0 11.6 1.0
NE2 A:HIS399 2.0 11.3 1.0
NE2 A:HIS111 2.1 12.9 1.0
O A:HOH3160 2.2 22.0 1.0
CE1 A:HIS399 2.8 11.8 1.0
CD2 A:HIS449 2.9 13.3 1.0
CE1 A:HIS111 3.0 10.3 1.0
CE1 A:HIS449 3.0 12.8 1.0
CD2 A:HIS399 3.1 10.4 1.0
CD2 A:HIS111 3.2 10.7 1.0
O A:HOH3077 3.8 19.9 1.0
CD2 A:HIS397 3.9 11.3 1.0
ND1 A:HIS399 4.0 10.2 1.0
CD2 A:PHE447 4.0 12.4 1.0
ND1 A:HIS449 4.1 11.6 1.0
CG A:HIS449 4.1 11.3 1.0
ND1 A:HIS111 4.1 11.8 1.0
CG A:HIS399 4.2 10.0 1.0
CG A:HIS111 4.2 10.3 1.0
CB A:PHE447 4.3 11.3 1.0
CG A:PRO79 4.5 12.2 1.0
CU A:CU1499 4.5 22.6 1.0
CG A:PHE447 4.6 11.1 1.0
CD2 A:HIS64 4.6 10.5 1.0
NE2 A:HIS397 4.7 11.5 1.0
NE2 A:HIS64 4.8 11.3 1.0
CE2 A:PHE447 4.9 13.2 1.0
NE2 A:HIS451 5.0 10.7 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: Sun Dec 13 11:05:08 2020

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