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Copper in PDB 6ril: Single Crystal Serial Study of the Inhibition of Laccases From Steccherinum Murashkinskyi By Fluoride Anions at Sub-Atomic Resolution. Fourteenth Structure of the Series with 5600 Kgy Dose (Data Was Collected After Refreezing).

Enzymatic activity of Single Crystal Serial Study of the Inhibition of Laccases From Steccherinum Murashkinskyi By Fluoride Anions at Sub-Atomic Resolution. Fourteenth Structure of the Series with 5600 Kgy Dose (Data Was Collected After Refreezing).

All present enzymatic activity of Single Crystal Serial Study of the Inhibition of Laccases From Steccherinum Murashkinskyi By Fluoride Anions at Sub-Atomic Resolution. Fourteenth Structure of the Series with 5600 Kgy Dose (Data Was Collected After Refreezing).:
1.10.3.2;

Protein crystallography data

The structure of Single Crystal Serial Study of the Inhibition of Laccases From Steccherinum Murashkinskyi By Fluoride Anions at Sub-Atomic Resolution. Fourteenth Structure of the Series with 5600 Kgy Dose (Data Was Collected After Refreezing)., PDB code: 6ril was solved by K.M.Polyakov, S.Gavryushov, T.V.Fedorova, O.A.Glazunova, A.N.Popov, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 67.43 / 1.34
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 56.190, 84.290, 112.390, 90.00, 90.00, 90.00
R / Rfree (%) 14 / 17.8

Other elements in 6ril:

The structure of Single Crystal Serial Study of the Inhibition of Laccases From Steccherinum Murashkinskyi By Fluoride Anions at Sub-Atomic Resolution. Fourteenth Structure of the Series with 5600 Kgy Dose (Data Was Collected After Refreezing). also contains other interesting chemical elements:

Fluorine (F) 2 atoms

Copper Binding Sites:

The binding sites of Copper atom in the Single Crystal Serial Study of the Inhibition of Laccases From Steccherinum Murashkinskyi By Fluoride Anions at Sub-Atomic Resolution. Fourteenth Structure of the Series with 5600 Kgy Dose (Data Was Collected After Refreezing). (pdb code 6ril). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 7 binding sites of Copper where determined in the Single Crystal Serial Study of the Inhibition of Laccases From Steccherinum Murashkinskyi By Fluoride Anions at Sub-Atomic Resolution. Fourteenth Structure of the Series with 5600 Kgy Dose (Data Was Collected After Refreezing)., PDB code: 6ril:
Jump to Copper binding site number: 1; 2; 3; 4; 5; 6; 7;

Copper binding site 1 out of 7 in 6ril

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Copper binding site 1 out of 7 in the Single Crystal Serial Study of the Inhibition of Laccases From Steccherinum Murashkinskyi By Fluoride Anions at Sub-Atomic Resolution. Fourteenth Structure of the Series with 5600 Kgy Dose (Data Was Collected After Refreezing).


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Single Crystal Serial Study of the Inhibition of Laccases From Steccherinum Murashkinskyi By Fluoride Anions at Sub-Atomic Resolution. Fourteenth Structure of the Series with 5600 Kgy Dose (Data Was Collected After Refreezing). within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu501

b:13.3
occ:0.65
CU A:CU501 0.0 13.3 0.7
CU A:CU501 0.8 11.8 0.3
NE2 A:HIS402 2.0 11.3 1.0
NE2 A:HIS112 2.0 10.6 1.0
NE2 A:HIS452 2.0 13.2 1.0
O A:HOH601 2.2 11.6 0.3
O1 A:OXY511 2.5 9.4 0.2
O2 A:OXY511 2.6 10.3 0.2
CE1 A:HIS402 2.8 11.8 1.0
CE1 A:HIS112 2.9 11.2 1.0
CD2 A:HIS452 2.9 11.9 1.0
HE1 A:HIS402 2.9 6.5 1.0
CE1 A:HIS452 3.0 13.1 1.0
HE1 A:HIS112 3.0 6.8 1.0
O A:HOH604 3.1 7.2 0.3
CD2 A:HIS402 3.1 12.0 1.0
CD2 A:HIS112 3.1 10.1 1.0
HD2 A:HIS452 3.1 10.4 1.0
HE1 A:HIS452 3.2 10.4 1.0
HD2 A:HIS400 3.3 6.9 1.0
HD2 A:PHE450 3.3 6.8 1.0
HD2 A:HIS112 3.3 6.8 1.0
HD2 A:HIS402 3.3 6.5 1.0
HB3 A:PHE450 3.6 6.5 1.0
ND1 A:HIS402 4.0 11.1 1.0
O A:HOH609 4.0 19.5 1.0
CD2 A:PHE450 4.0 12.6 1.0
CG A:HIS452 4.0 12.0 1.0
ND1 A:HIS452 4.1 11.5 1.0
ND1 A:HIS112 4.1 12.7 1.0
HB3 A:PRO80 4.1 6.0 1.0
CG A:HIS402 4.1 10.8 1.0
CD2 A:HIS400 4.2 11.2 1.0
HE1 A:HIS110 4.2 10.5 1.0
CG A:HIS112 4.2 10.7 1.0
CU A:CU503 4.3 11.0 0.5
CU A:CU503 4.3 11.4 0.3
HD2 A:HIS65 4.3 9.1 1.0
CD2 A:HIS65 4.4 10.9 1.0
CB A:PHE450 4.4 11.3 1.0
NE2 A:HIS65 4.4 9.9 1.0
CU A:CU502 4.5 13.0 0.3
HB2 A:PHE450 4.5 6.5 1.0
HD21 A:LEU459 4.6 7.7 1.0
CG A:PHE450 4.6 12.1 1.0
HD1 A:HIS402 4.7 6.5 1.0
NE2 A:HIS400 4.7 10.6 1.0
HE2 A:PHE450 4.8 6.8 1.0
CE2 A:PHE450 4.8 14.4 1.0
HD1 A:HIS112 4.8 6.8 1.0
HD1 A:HIS452 4.8 10.4 1.0
HD22 A:LEU459 5.0 7.7 1.0
HD2 A:HIS454 5.0 6.4 1.0
CE1 A:HIS110 5.0 10.7 1.0

Copper binding site 2 out of 7 in 6ril

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Copper binding site 2 out of 7 in the Single Crystal Serial Study of the Inhibition of Laccases From Steccherinum Murashkinskyi By Fluoride Anions at Sub-Atomic Resolution. Fourteenth Structure of the Series with 5600 Kgy Dose (Data Was Collected After Refreezing).


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of Single Crystal Serial Study of the Inhibition of Laccases From Steccherinum Murashkinskyi By Fluoride Anions at Sub-Atomic Resolution. Fourteenth Structure of the Series with 5600 Kgy Dose (Data Was Collected After Refreezing). within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu501

b:11.8
occ:0.30
CU A:CU501 0.0 11.8 0.3
CU A:CU501 0.8 13.3 0.7
O A:HOH601 1.5 11.6 0.3
O2 A:OXY511 1.8 10.3 0.2
O1 A:OXY511 1.9 9.4 0.2
NE2 A:HIS402 2.2 11.3 1.0
NE2 A:HIS452 2.2 13.2 1.0
NE2 A:HIS112 2.2 10.6 1.0
O A:HOH604 2.4 7.2 0.3
HD2 A:HIS400 2.9 6.9 1.0
CE1 A:HIS452 3.0 13.1 1.0
HE1 A:HIS452 3.0 10.4 1.0
CE1 A:HIS402 3.0 11.8 1.0
CD2 A:HIS112 3.1 10.1 1.0
HE1 A:HIS402 3.2 6.5 1.0
HD2 A:HIS112 3.2 6.8 1.0
CD2 A:HIS402 3.2 12.0 1.0
CE1 A:HIS112 3.3 11.2 1.0
CD2 A:HIS452 3.3 11.9 1.0
HD2 A:HIS402 3.4 6.5 1.0
HE1 A:HIS112 3.6 6.8 1.0
HD2 A:HIS452 3.6 10.4 1.0
HE1 A:HIS110 3.7 10.5 1.0
O A:HOH609 3.7 19.5 1.0
CU A:CU502 3.7 13.0 0.3
CD2 A:HIS400 3.7 11.2 1.0
HD2 A:HIS65 3.7 9.1 1.0
CU A:CU503 3.8 11.0 0.5
CU A:CU503 3.8 11.4 0.3
CD2 A:HIS65 3.9 10.9 1.0
NE2 A:HIS65 4.0 9.9 1.0
HD2 A:PHE450 4.1 6.8 1.0
ND1 A:HIS452 4.2 11.5 1.0
ND1 A:HIS402 4.2 11.1 1.0
HB3 A:PHE450 4.2 6.5 1.0
CG A:HIS402 4.3 10.8 1.0
NE2 A:HIS400 4.3 10.6 1.0
CG A:HIS112 4.3 10.7 1.0
CG A:HIS452 4.4 12.0 1.0
ND1 A:HIS112 4.4 12.7 1.0
NE2 A:HIS454 4.4 10.8 1.0
HD2 A:HIS454 4.4 6.4 1.0
CU A:CU502 4.4 10.8 0.7
CE1 A:HIS110 4.4 10.7 1.0
CD2 A:HIS454 4.6 10.5 1.0
HB3 A:PRO80 4.6 6.0 1.0
CD2 A:PHE450 4.7 12.6 1.0
CG A:HIS65 4.8 12.0 1.0
CE1 A:HIS65 4.8 10.4 1.0
NE2 A:HIS110 4.8 10.1 1.0
HD21 A:LEU459 4.8 7.7 1.0
HD1 A:HIS452 4.9 10.4 1.0
HD1 A:HIS402 4.9 6.5 1.0
CG A:HIS400 5.0 10.7 1.0

Copper binding site 3 out of 7 in 6ril

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Copper binding site 3 out of 7 in the Single Crystal Serial Study of the Inhibition of Laccases From Steccherinum Murashkinskyi By Fluoride Anions at Sub-Atomic Resolution. Fourteenth Structure of the Series with 5600 Kgy Dose (Data Was Collected After Refreezing).


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 3 of Single Crystal Serial Study of the Inhibition of Laccases From Steccherinum Murashkinskyi By Fluoride Anions at Sub-Atomic Resolution. Fourteenth Structure of the Series with 5600 Kgy Dose (Data Was Collected After Refreezing). within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu502

b:10.8
occ:0.65
CU A:CU502 0.0 10.8 0.7
CU A:CU502 0.7 13.0 0.3
ND1 A:HIS67 1.9 11.4 1.0
NE2 A:HIS110 2.0 10.1 1.0
NE2 A:HIS454 2.1 10.8 1.0
O2 A:OXY511 2.6 10.3 0.2
O A:HOH604 2.7 7.2 0.3
HB2 A:HIS67 2.7 4.7 1.0
CE1 A:HIS67 2.9 10.8 1.0
CG A:HIS67 2.9 10.5 1.0
CD2 A:HIS110 3.0 10.3 1.0
CE1 A:HIS454 3.0 12.4 1.0
CE1 A:HIS110 3.1 10.7 1.0
HE1 A:HIS67 3.1 6.5 1.0
HE1 A:HIS454 3.1 6.4 1.0
HD2 A:HIS110 3.1 10.5 1.0
O A:HOH601 3.2 11.6 0.3
HD2 A:HIS65 3.2 9.1 1.0
CD2 A:HIS454 3.2 10.5 1.0
CB A:HIS67 3.3 9.6 1.0
HE1 A:HIS110 3.3 10.5 1.0
O1 A:OXY511 3.3 9.4 0.2
HZ2 A:TRP108 3.4 6.6 1.0
HD2 A:HIS454 3.5 6.4 1.0
HB2 A:ALA244 3.5 6.6 1.0
CZ2 A:TRP108 3.7 10.9 1.0
HB3 A:HIS67 3.9 4.7 1.0
HE1 A:TRP108 3.9 6.6 1.0
CE2 A:TRP108 3.9 9.7 1.0
CD2 A:HIS65 3.9 10.9 1.0
NE2 A:HIS67 3.9 12.1 1.0
CU A:CU503 4.0 11.0 0.5
CU A:CU503 4.0 11.4 0.3
CD2 A:HIS67 4.0 10.3 1.0
NE1 A:TRP108 4.1 10.4 1.0
CG A:HIS110 4.2 10.7 1.0
ND1 A:HIS454 4.2 11.6 1.0
ND1 A:HIS110 4.2 10.4 1.0
NE2 A:HIS65 4.2 9.9 1.0
HD2 A:HIS400 4.2 6.9 1.0
HB1 A:ALA244 4.3 6.6 1.0
HA A:HIS67 4.3 3.8 1.0
CG A:HIS454 4.3 10.2 1.0
CB A:ALA244 4.3 10.9 1.0
CD2 A:HIS400 4.4 11.2 1.0
CU A:CU501 4.4 11.8 0.3
CA A:HIS67 4.4 9.9 1.0
CH2 A:TRP108 4.5 10.1 1.0
NE2 A:HIS400 4.5 10.6 1.0
O A:HOH609 4.6 19.5 1.0
HH2 A:TRP108 4.7 6.6 1.0
HE2 A:HIS67 4.7 6.5 1.0
HB3 A:ALA244 4.7 6.6 1.0
CD2 A:TRP108 4.8 9.8 1.0
HD2 A:HIS67 4.9 6.5 1.0
HD1 A:HIS454 4.9 6.4 1.0
HD1 A:HIS110 4.9 10.5 1.0
HE1 A:HIS452 4.9 10.4 1.0
CD1 A:TRP108 5.0 10.8 1.0

Copper binding site 4 out of 7 in 6ril

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Copper binding site 4 out of 7 in the Single Crystal Serial Study of the Inhibition of Laccases From Steccherinum Murashkinskyi By Fluoride Anions at Sub-Atomic Resolution. Fourteenth Structure of the Series with 5600 Kgy Dose (Data Was Collected After Refreezing).


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 4 of Single Crystal Serial Study of the Inhibition of Laccases From Steccherinum Murashkinskyi By Fluoride Anions at Sub-Atomic Resolution. Fourteenth Structure of the Series with 5600 Kgy Dose (Data Was Collected After Refreezing). within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu502

b:13.0
occ:0.30
CU A:CU502 0.0 13.0 0.3
CU A:CU502 0.7 10.8 0.7
O2 A:OXY511 1.9 10.3 0.2
NE2 A:HIS454 2.1 10.8 1.0
NE2 A:HIS110 2.1 10.1 1.0
O A:HOH604 2.1 7.2 0.3
ND1 A:HIS67 2.2 11.4 1.0
O A:HOH601 2.5 11.6 0.3
O1 A:OXY511 2.7 9.4 0.2
CE1 A:HIS110 2.9 10.7 1.0
HD2 A:HIS65 2.9 9.1 1.0
HE1 A:HIS110 2.9 10.5 1.0
CE1 A:HIS454 3.0 12.4 1.0
CD2 A:HIS454 3.1 10.5 1.0
HB2 A:HIS67 3.1 4.7 1.0
CE1 A:HIS67 3.1 10.8 1.0
HE1 A:HIS454 3.2 6.4 1.0
HE1 A:HIS67 3.2 6.5 1.0
HD2 A:HIS454 3.2 6.4 1.0
CD2 A:HIS110 3.3 10.3 1.0
CG A:HIS67 3.3 10.5 1.0
CD2 A:HIS65 3.6 10.9 1.0
HD2 A:HIS110 3.6 10.5 1.0
CU A:CU503 3.7 11.0 0.5
CU A:CU503 3.7 11.4 0.3
CU A:CU501 3.7 11.8 0.3
CB A:HIS67 3.7 9.6 1.0
HD2 A:HIS400 3.7 6.9 1.0
NE2 A:HIS65 3.9 9.9 1.0
CD2 A:HIS400 4.0 11.2 1.0
HB2 A:ALA244 4.0 6.6 1.0
HZ2 A:TRP108 4.0 6.6 1.0
ND1 A:HIS110 4.1 10.4 1.0
O A:HOH609 4.1 19.5 1.0
ND1 A:HIS454 4.1 11.6 1.0
CG A:HIS454 4.2 10.2 1.0
NE2 A:HIS400 4.2 10.6 1.0
NE2 A:HIS67 4.3 12.1 1.0
CZ2 A:TRP108 4.3 10.9 1.0
CG A:HIS110 4.3 10.7 1.0
HA A:HIS67 4.4 3.8 1.0
HE1 A:HIS452 4.4 10.4 1.0
HB3 A:HIS67 4.4 4.7 1.0
CD2 A:HIS67 4.4 10.3 1.0
CU A:CU501 4.5 13.3 0.7
HD2 A:HIS112 4.5 6.8 1.0
HE1 A:TRP108 4.6 6.6 1.0
HB1 A:ALA244 4.6 6.6 1.0
CE2 A:TRP108 4.6 9.7 1.0
CA A:HIS67 4.7 9.9 1.0
CB A:ALA244 4.7 10.9 1.0
NE1 A:TRP108 4.8 10.4 1.0
HD1 A:HIS110 4.8 10.5 1.0
CG A:HIS65 4.9 12.0 1.0
CG A:HIS400 4.9 10.7 1.0
HD1 A:HIS454 4.9 6.4 1.0
CD2 A:HIS112 5.0 10.1 1.0
CH2 A:TRP108 5.0 10.1 1.0

Copper binding site 5 out of 7 in 6ril

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Copper binding site 5 out of 7 in the Single Crystal Serial Study of the Inhibition of Laccases From Steccherinum Murashkinskyi By Fluoride Anions at Sub-Atomic Resolution. Fourteenth Structure of the Series with 5600 Kgy Dose (Data Was Collected After Refreezing).


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 5 of Single Crystal Serial Study of the Inhibition of Laccases From Steccherinum Murashkinskyi By Fluoride Anions at Sub-Atomic Resolution. Fourteenth Structure of the Series with 5600 Kgy Dose (Data Was Collected After Refreezing). within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu503

b:11.0
occ:0.53
CU A:CU503 0.0 11.0 0.5
CU A:CU503 0.0 11.4 0.3
F A:F509 1.6 9.8 0.3
NE2 A:HIS65 1.9 9.9 1.0
NE2 A:HIS400 1.9 10.6 1.0
O A:HOH604 2.0 7.2 0.3
O A:HOH618 2.3 8.6 0.2
F A:F509 2.5 12.2 0.5
CE1 A:HIS65 2.7 10.4 1.0
CD2 A:HIS400 2.8 11.2 1.0
HE1 A:HIS65 2.9 9.5 1.0
CE1 A:HIS400 3.0 11.5 1.0
HD2 A:HIS400 3.0 6.9 1.0
HA A:HIS67 3.0 3.8 1.0
CD2 A:HIS65 3.1 10.9 1.0
H A:GLY68 3.2 3.8 1.0
CD2 A:HIS402 3.2 12.0 1.0
HE1 A:HIS400 3.2 6.9 1.0
NE2 A:HIS402 3.3 11.3 1.0
HD2 A:HIS65 3.4 9.1 1.0
HD2 A:HIS402 3.4 6.5 1.0
O2 A:OXY511 3.4 10.3 0.2
ND1 A:HIS67 3.5 11.4 1.0
HA A:HIS402 3.6 12.2 1.0
CU A:CU502 3.7 13.0 0.3
CG A:HIS402 3.7 10.8 1.0
CU A:CU501 3.8 11.8 0.3
CG A:HIS67 3.8 10.5 1.0
CE1 A:HIS402 3.8 11.8 1.0
CA A:HIS67 3.9 9.9 1.0
CE1 A:HIS67 3.9 10.8 1.0
ND1 A:HIS65 3.9 11.7 1.0
ND1 A:HIS402 4.0 11.1 1.0
N A:GLY68 4.0 9.5 1.0
CU A:CU502 4.0 10.8 0.7
CG A:HIS400 4.0 10.7 1.0
O A:HOH601 4.0 11.6 0.3
ND1 A:HIS400 4.0 11.4 1.0
HB2 A:HIS67 4.1 4.7 1.0
CG A:HIS65 4.1 12.0 1.0
CB A:HIS67 4.1 9.6 1.0
HE1 A:HIS67 4.2 6.5 1.0
CU A:CU501 4.3 13.3 0.7
HE1 A:HIS402 4.3 6.5 1.0
CD2 A:HIS67 4.3 10.3 1.0
CA A:HIS402 4.3 11.6 1.0
NE2 A:HIS67 4.4 12.1 1.0
CB A:HIS402 4.5 10.8 1.0
C A:HIS67 4.5 9.9 1.0
O A:HOH731 4.5 16.4 1.0
HD1 A:HIS402 4.6 6.5 1.0
O1 A:OXY511 4.6 9.4 0.2
O A:HOH890 4.7 14.1 1.0
HD1 A:HIS65 4.7 9.3 1.0
HB3 A:HIS402 4.7 6.6 1.0
N A:HIS402 4.8 10.6 1.0
HD1 A:HIS400 4.8 6.9 1.0
HA2 A:GLY68 4.9 5.5 1.0
HD2 A:HIS67 4.9 6.5 1.0
HE2 A:HIS67 4.9 6.5 1.0
HD2 A:HIS112 4.9 6.8 1.0
HD2 A:HIS454 4.9 6.4 1.0
O A:LEU401 4.9 10.7 1.0
N A:HIS67 5.0 8.9 1.0

Copper binding site 6 out of 7 in 6ril

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Copper binding site 6 out of 7 in the Single Crystal Serial Study of the Inhibition of Laccases From Steccherinum Murashkinskyi By Fluoride Anions at Sub-Atomic Resolution. Fourteenth Structure of the Series with 5600 Kgy Dose (Data Was Collected After Refreezing).


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 6 of Single Crystal Serial Study of the Inhibition of Laccases From Steccherinum Murashkinskyi By Fluoride Anions at Sub-Atomic Resolution. Fourteenth Structure of the Series with 5600 Kgy Dose (Data Was Collected After Refreezing). within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu503

b:11.4
occ:0.30
CU A:CU503 0.0 11.4 0.3
CU A:CU503 0.0 11.0 0.5
F A:F509 1.6 9.8 0.3
NE2 A:HIS65 1.9 9.9 1.0
NE2 A:HIS400 1.9 10.6 1.0
O A:HOH604 2.0 7.2 0.3
O A:HOH618 2.3 8.6 0.2
F A:F509 2.5 12.2 0.5
CE1 A:HIS65 2.7 10.4 1.0
CD2 A:HIS400 2.8 11.2 1.0
HE1 A:HIS65 2.9 9.5 1.0
CE1 A:HIS400 3.0 11.5 1.0
HD2 A:HIS400 3.0 6.9 1.0
HA A:HIS67 3.0 3.8 1.0
CD2 A:HIS65 3.1 10.9 1.0
H A:GLY68 3.2 3.8 1.0
CD2 A:HIS402 3.2 12.0 1.0
HE1 A:HIS400 3.2 6.9 1.0
NE2 A:HIS402 3.4 11.3 1.0
HD2 A:HIS65 3.4 9.1 1.0
HD2 A:HIS402 3.4 6.5 1.0
O2 A:OXY511 3.4 10.3 0.2
ND1 A:HIS67 3.5 11.4 1.0
HA A:HIS402 3.6 12.2 1.0
CU A:CU502 3.7 13.0 0.3
CG A:HIS402 3.7 10.8 1.0
CG A:HIS67 3.8 10.5 1.0
CU A:CU501 3.8 11.8 0.3
CE1 A:HIS402 3.8 11.8 1.0
CA A:HIS67 3.9 9.9 1.0
CE1 A:HIS67 3.9 10.8 1.0
ND1 A:HIS65 3.9 11.7 1.0
ND1 A:HIS402 4.0 11.1 1.0
N A:GLY68 4.0 9.5 1.0
CU A:CU502 4.0 10.8 0.7
CG A:HIS400 4.0 10.7 1.0
O A:HOH601 4.0 11.6 0.3
ND1 A:HIS400 4.0 11.4 1.0
HB2 A:HIS67 4.1 4.7 1.0
CG A:HIS65 4.1 12.0 1.0
CB A:HIS67 4.1 9.6 1.0
HE1 A:HIS67 4.2 6.5 1.0
CU A:CU501 4.3 13.3 0.7
HE1 A:HIS402 4.3 6.5 1.0
CD2 A:HIS67 4.3 10.3 1.0
CA A:HIS402 4.3 11.6 1.0
NE2 A:HIS67 4.4 12.1 1.0
CB A:HIS402 4.5 10.8 1.0
C A:HIS67 4.5 9.9 1.0
O A:HOH731 4.5 16.4 1.0
HD1 A:HIS402 4.6 6.5 1.0
O1 A:OXY511 4.6 9.4 0.2
O A:HOH890 4.7 14.1 1.0
HD1 A:HIS65 4.7 9.3 1.0
HB3 A:HIS402 4.7 6.6 1.0
N A:HIS402 4.8 10.6 1.0
HD1 A:HIS400 4.8 6.9 1.0
HA2 A:GLY68 4.9 5.5 1.0
HD2 A:HIS67 4.9 6.5 1.0
HE2 A:HIS67 4.9 6.5 1.0
HD2 A:HIS112 4.9 6.8 1.0
HD2 A:HIS454 4.9 6.4 1.0
O A:LEU401 4.9 10.7 1.0
N A:HIS67 5.0 8.9 1.0

Copper binding site 7 out of 7 in 6ril

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Copper binding site 7 out of 7 in the Single Crystal Serial Study of the Inhibition of Laccases From Steccherinum Murashkinskyi By Fluoride Anions at Sub-Atomic Resolution. Fourteenth Structure of the Series with 5600 Kgy Dose (Data Was Collected After Refreezing).


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 7 of Single Crystal Serial Study of the Inhibition of Laccases From Steccherinum Murashkinskyi By Fluoride Anions at Sub-Atomic Resolution. Fourteenth Structure of the Series with 5600 Kgy Dose (Data Was Collected After Refreezing). within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu504

b:10.9
occ:0.85
ND1 A:HIS397 2.0 11.7 1.0
ND1 A:HIS458 2.0 11.7 1.0
SG A:CYS453 2.2 12.2 1.0
HD11 A:ILE455 2.6 6.3 1.0
CE1 A:HIS397 2.9 12.3 1.0
HB A:ILE455 2.9 6.3 1.0
CE1 A:HIS458 3.0 12.0 1.0
HB3 A:HIS397 3.0 9.1 1.0
HE1 A:HIS397 3.1 6.2 1.0
HD2 A:PHE463 3.1 9.4 1.0
CG A:HIS458 3.1 11.6 1.0
CG A:HIS397 3.1 12.1 1.0
HB2 A:HIS458 3.1 6.3 1.0
HE1 A:HIS458 3.1 6.2 1.0
HB3 A:HIS458 3.3 6.3 1.0
CB A:CYS453 3.3 12.4 1.0
CB A:HIS458 3.4 11.3 1.0
HB2 A:CYS453 3.4 5.3 1.0
HA A:HIS397 3.4 6.3 1.0
HB3 A:CYS453 3.4 5.3 1.0
CB A:HIS397 3.5 11.8 1.0
CD1 A:ILE455 3.5 11.3 1.0
HE2 A:PHE463 3.5 9.4 1.0
HD2 A:PRO398 3.8 6.3 1.0
CB A:ILE455 3.8 11.3 1.0
CD2 A:PHE463 3.8 11.3 1.0
HD12 A:ILE455 3.9 6.3 1.0
H A:ILE455 3.9 6.3 1.0
CA A:HIS397 4.0 11.6 1.0
CG1 A:ILE455 4.0 11.3 1.0
HG13 A:ILE455 4.0 6.3 1.0
CE2 A:PHE463 4.1 11.0 1.0
NE2 A:HIS397 4.1 12.3 1.0
NE2 A:HIS458 4.1 12.8 1.0
HD13 A:ILE455 4.1 6.3 1.0
CD2 A:HIS458 4.2 12.7 1.0
CD2 A:HIS397 4.2 13.3 1.0
HB2 A:HIS397 4.3 9.1 1.0
HG22 A:ILE455 4.5 6.3 1.0
CG2 A:ILE455 4.6 11.5 1.0
CD A:PRO398 4.6 11.8 1.0
HZ A:PHE341 4.6 8.8 1.0
HG21 A:ILE455 4.6 6.3 1.0
CA A:CYS453 4.6 11.5 1.0
O A:GLY394 4.7 14.4 1.0
CZ A:PHE341 4.8 13.2 1.0
N A:ILE455 4.8 10.3 1.0
HD3 A:PRO398 4.8 6.3 1.0
HA A:CYS453 4.8 4.8 1.0
HE2 A:HIS397 4.8 6.2 1.0
HA2 A:GLY395 4.9 8.9 1.0
HE2 A:PHE341 4.9 8.8 1.0
CA A:ILE455 4.9 11.1 1.0
HE1 A:PHE399 4.9 9.0 1.0
CA A:HIS458 4.9 11.1 1.0
HE2 A:HIS458 4.9 6.2 1.0
CE2 A:PHE341 4.9 12.2 1.0
C A:HIS397 4.9 11.9 1.0
O A:ILE455 4.9 11.2 1.0
HG12 A:ILE455 4.9 6.3 1.0
N A:HIS397 5.0 11.7 1.0
HB3 A:PHE463 5.0 6.4 1.0

Reference:

K.M.Polyakov, S.Gavryushov, T.V.Fedorova, O.A.Glazunova, A.N.Popov. The Subatomic Resolution Study of Laccase Inhibition By Chloride and Fluoride Anions Using Single-Crystal Serial Crystallography: Insights Into the Enzymatic Reaction Mechanism. Acta Crystallogr D Struct V. 75 804 2019BIOL.
ISSN: ISSN 2059-7983
PubMed: 31478903
DOI: 10.1107/S2059798319010684
Page generated: Sun Dec 13 11:25:40 2020

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