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Copper in PDB 3fpx: Native Fungus Laccase From Trametes Hirsuta

Enzymatic activity of Native Fungus Laccase From Trametes Hirsuta

All present enzymatic activity of Native Fungus Laccase From Trametes Hirsuta:
1.10.3.2;

Protein crystallography data

The structure of Native Fungus Laccase From Trametes Hirsuta, PDB code: 3fpx was solved by K.M.Polyakov, T.V.Fedorova, E.V.Stepanova, E.A.Cherkashin, S.A.Kurzeev, B.V.Strokopytov, V.S.Lamzin, O.V.Koroleva, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 65.90 / 1.80
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 52.293, 76.345, 129.661, 90.00, 90.00, 90.00
R / Rfree (%) 18 / 23.3

Copper Binding Sites:

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

Copper binding site 1 out of 4 in 3fpx

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Copper binding site 1 out of 4 in the Native Fungus Laccase From Trametes Hirsuta


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Native Fungus Laccase From Trametes Hirsuta within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu1500

b:24.6
occ:0.70
O A:HOH1000 1.7 22.1 0.8
NE2 A:HIS400 2.0 21.4 1.0
NE2 A:HIS111 2.0 20.3 1.0
NE2 A:HIS452 2.0 19.6 1.0
O A:HOH1001 2.7 24.6 0.8
CE1 A:HIS400 2.8 18.0 1.0
CE1 A:HIS452 2.9 23.0 1.0
CE1 A:HIS111 3.0 24.4 1.0
CD2 A:HIS111 3.0 20.8 1.0
CD2 A:HIS452 3.1 21.4 1.0
CD2 A:HIS400 3.2 23.8 1.0
CD2 A:HIS398 3.6 23.6 1.0
O A:HOH1002 3.6 26.6 0.8
CU A:CU1501 3.8 31.4 0.7
ND1 A:HIS400 4.0 21.6 1.0
ND1 A:HIS452 4.1 22.7 1.0
CU A:CU1502 4.1 26.8 0.7
ND1 A:HIS111 4.1 22.0 1.0
CD2 A:HIS64 4.2 21.3 1.0
CG A:HIS111 4.2 23.9 1.0
CG A:HIS400 4.2 21.4 1.0
CG A:HIS452 4.2 18.4 1.0
NE2 A:HIS398 4.3 20.8 1.0
NE2 A:HIS64 4.3 22.1 1.0
NE2 A:HIS454 4.4 23.1 1.0
CE1 A:HIS109 4.4 22.9 1.0
CD2 A:HIS454 4.6 24.5 1.0
NE2 A:HIS109 4.7 22.9 1.0
CD2 A:PHE450 4.7 22.5 1.0
CG A:HIS398 4.8 20.1 1.0
CG A:HIS64 4.9 20.1 1.0

Copper binding site 2 out of 4 in 3fpx

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Copper binding site 2 out of 4 in the Native Fungus Laccase From Trametes Hirsuta


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of Native Fungus Laccase From Trametes Hirsuta within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu1501

b:31.4
occ:0.70
NE2 A:HIS454 2.0 23.1 1.0
ND1 A:HIS66 2.0 21.4 1.0
NE2 A:HIS109 2.1 22.9 1.0
O A:HOH1001 2.2 24.6 0.8
O A:HOH1000 2.4 22.1 0.8
CE1 A:HIS66 2.9 19.0 1.0
CE1 A:HIS454 2.9 22.6 1.0
CE1 A:HIS109 3.0 22.9 1.0
CD2 A:HIS454 3.1 24.5 1.0
CG A:HIS66 3.2 22.1 1.0
CD2 A:HIS109 3.2 23.2 1.0
CB A:HIS66 3.6 20.7 1.0
CD2 A:HIS64 3.7 21.3 1.0
CU A:CU1502 3.8 26.8 0.7
CU A:CU1500 3.8 24.6 0.7
CD2 A:HIS398 3.9 23.6 1.0
NE2 A:HIS66 4.1 20.3 1.0
ND1 A:HIS454 4.1 23.4 1.0
NE2 A:HIS398 4.1 20.8 1.0
CZ2 A:TRP107 4.1 20.4 1.0
ND1 A:HIS109 4.1 21.9 1.0
NE2 A:HIS64 4.1 22.1 1.0
CG A:HIS454 4.2 24.1 1.0
CD2 A:HIS66 4.2 21.4 1.0
O A:HOH1002 4.3 26.6 0.8
CG A:HIS109 4.3 22.5 1.0
CE2 A:TRP107 4.4 22.5 1.0
NE1 A:TRP107 4.5 21.6 1.0
CB A:ALA241 4.6 22.5 1.0
CA A:HIS66 4.7 20.8 1.0
CG A:HIS398 4.8 20.1 1.0
NE2 A:HIS111 4.9 20.3 1.0
CH2 A:TRP107 4.9 22.1 1.0
CD2 A:HIS111 4.9 20.8 1.0
CG A:HIS64 4.9 20.1 1.0
CE1 A:HIS398 5.0 22.3 1.0

Copper binding site 3 out of 4 in 3fpx

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Copper binding site 3 out of 4 in the Native Fungus Laccase From Trametes Hirsuta


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 3 of Native Fungus Laccase From Trametes Hirsuta within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu1502

b:26.8
occ:0.70
NE2 A:HIS398 1.8 20.8 1.0
O A:HOH1001 2.0 24.6 0.8
NE2 A:HIS64 2.0 22.1 1.0
O A:HOH1003 2.1 20.8 0.9
CE1 A:HIS398 2.8 22.3 1.0
CD2 A:HIS398 2.8 23.6 1.0
CE1 A:HIS64 2.9 23.1 1.0
CD2 A:HIS64 3.0 21.3 1.0
ND1 A:HIS66 3.4 21.4 1.0
CE1 A:HIS400 3.4 18.0 1.0
NE2 A:HIS400 3.5 21.4 1.0
CG A:HIS66 3.6 22.1 1.0
ND1 A:HIS400 3.6 21.6 1.0
CD2 A:HIS400 3.6 23.8 1.0
CG A:HIS400 3.7 21.4 1.0
CE1 A:HIS66 3.8 19.0 1.0
CU A:CU1501 3.8 31.4 0.7
CA A:HIS66 3.8 20.8 1.0
ND1 A:HIS398 3.9 27.2 1.0
N A:GLY67 3.9 20.1 1.0
CG A:HIS398 4.0 20.1 1.0
CD2 A:HIS66 4.0 21.4 1.0
CB A:HIS66 4.0 20.7 1.0
ND1 A:HIS64 4.0 21.8 1.0
CG A:HIS64 4.1 20.1 1.0
CU A:CU1500 4.1 24.6 0.7
NE2 A:HIS66 4.1 20.3 1.0
O A:HOH1000 4.3 22.1 0.8
O A:HOH1018 4.4 22.8 1.0
O A:HOH1024 4.4 24.9 1.0
CA A:HIS400 4.4 21.3 1.0
C A:HIS66 4.4 20.4 1.0
CB A:HIS400 4.5 20.4 1.0
N A:HIS400 4.9 20.9 1.0
N A:HIS66 4.9 19.3 1.0
CA A:GLY67 5.0 21.5 1.0

Copper binding site 4 out of 4 in 3fpx

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Copper binding site 4 out of 4 in the Native Fungus Laccase From Trametes Hirsuta


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 4 of Native Fungus Laccase From Trametes Hirsuta within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu1503

b:27.4
occ:0.80
ND1 A:HIS395 2.0 27.1 1.0
ND1 A:HIS458 2.0 24.1 1.0
SG A:CYS453 2.2 23.8 1.0
CE1 A:HIS395 2.9 25.5 1.0
CE1 A:HIS458 3.0 25.0 1.0
CG A:HIS458 3.1 22.0 1.0
CG A:HIS395 3.1 23.4 1.0
CB A:CYS453 3.3 21.9 1.0
CB A:HIS458 3.4 23.0 1.0
CD1 A:ILE455 3.5 21.6 1.0
CB A:HIS395 3.5 25.2 1.0
CD2 A:PHE463 3.6 22.6 1.0
CE2 A:PHE463 3.8 20.0 1.0
CB A:ILE455 3.9 23.0 1.0
CA A:HIS395 4.0 24.5 1.0
NE2 A:HIS395 4.0 25.4 1.0
NE2 A:HIS458 4.1 25.2 1.0
CD2 A:HIS458 4.2 23.6 1.0
CD2 A:HIS395 4.2 25.7 1.0
CG1 A:ILE455 4.2 21.8 1.0
O A:GLY392 4.5 31.8 1.0
CD A:PRO396 4.6 22.5 1.0
CA A:CYS453 4.7 22.4 1.0
CG2 A:ILE455 4.7 21.4 1.0
N A:ILE455 4.8 23.3 1.0
CA A:HIS458 4.9 22.9 1.0
CA A:ILE455 4.9 22.3 1.0
CG A:PHE463 4.9 20.9 1.0
N A:HIS395 5.0 23.7 1.0
CZ A:PHE337 5.0 24.2 1.0

Reference:

K.M.Polyakov, T.V.Fedorova, E.V.Stepanova, E.A.Cherkashin, S.A.Kurzeev, B.V.Strokopytov, V.S.Lamzin, O.V.Koroleva. Structure of Native Laccase From Coriolus Hirsutus at 1.8 A Resolution To Be Published.
Page generated: Wed Oct 28 14:23:52 2020
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