Atomistry » Copper » PDB 6ri0-6vbs » 6ri6
Atomistry »
  Copper »
    PDB 6ri0-6vbs »
      6ri6 »

Copper in PDB 6ri6: Single Crystal Serial Study of the Inhibition of Laccases From Steccherinum Murashkinskyi By Fluoride Anions at Sub-Atomic Resolution. Second Structure of the Series with 400 Kgy Dose.

Enzymatic activity of Single Crystal Serial Study of the Inhibition of Laccases From Steccherinum Murashkinskyi By Fluoride Anions at Sub-Atomic Resolution. Second Structure of the Series with 400 Kgy Dose.

All present enzymatic activity of Single Crystal Serial Study of the Inhibition of Laccases From Steccherinum Murashkinskyi By Fluoride Anions at Sub-Atomic Resolution. Second Structure of the Series with 400 Kgy Dose.:
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. Second Structure of the Series with 400 Kgy Dose., PDB code: 6ri6 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) 67.34 / 0.93
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 56.150, 84.180, 112.200, 90.00, 90.00, 90.00
R / Rfree (%) 10.6 / 11.7

Other elements in 6ri6:

The structure of Single Crystal Serial Study of the Inhibition of Laccases From Steccherinum Murashkinskyi By Fluoride Anions at Sub-Atomic Resolution. Second Structure of the Series with 400 Kgy Dose. 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. Second Structure of the Series with 400 Kgy Dose. (pdb code 6ri6). 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. Second Structure of the Series with 400 Kgy Dose., PDB code: 6ri6:
Jump to Copper binding site number: 1; 2; 3; 4; 5; 6; 7;

Copper binding site 1 out of 7 in 6ri6

Go back to Copper Binding Sites List in 6ri6
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. Second Structure of the Series with 400 Kgy Dose.


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. Second Structure of the Series with 400 Kgy Dose. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu501

b:8.2
occ:0.55
CU A:CU501 0.0 8.2 0.6
CU A:CU501 0.8 5.3 0.4
NE2 A:HIS452 1.9 9.5 1.0
NE2 A:HIS402 1.9 6.3 1.0
NE2 A:HIS112 2.0 7.4 1.0
O1 A:OXY512 2.4 8.6 0.2
O A:HOH601 2.5 8.4 0.5
O2 A:OXY512 2.5 9.1 0.2
CD2 A:HIS452 2.8 8.7 1.0
CE1 A:HIS402 2.8 6.4 1.0
CE1 A:HIS112 2.9 8.0 1.0
CE1 A:HIS452 2.9 8.2 1.0
O A:HOH608 2.9 5.1 0.4
HD2 A:HIS452 3.0 8.5 1.0
HE1 A:HIS112 3.0 7.9 1.0
HE1 A:HIS402 3.0 7.3 1.0
CD2 A:HIS402 3.0 6.1 1.0
CD2 A:HIS112 3.1 6.7 1.0
HD2 A:PHE450 3.2 7.9 1.0
HE1 A:HIS452 3.2 8.5 1.0
HD2 A:HIS402 3.2 7.3 1.0
HD2 A:HIS112 3.4 7.9 1.0
HD2 A:HIS400 3.4 5.2 1.0
HB3 A:PHE450 3.6 7.3 1.0
O A:HOH613 3.6 5.5 0.2
CD2 A:PHE450 3.9 7.0 1.0
CG A:HIS452 3.9 7.4 1.0
ND1 A:HIS452 4.0 7.5 1.0
O A:HOH614 4.0 12.2 0.8
ND1 A:HIS402 4.0 6.3 1.0
ND1 A:HIS112 4.1 7.3 1.0
HB3 A:PRO80 4.1 7.1 1.0
CG A:HIS402 4.1 6.0 1.0
CG A:HIS112 4.2 6.3 1.0
CD2 A:HIS400 4.2 6.5 1.0
HE1 A:HIS110 4.2 8.7 1.0
HD2 A:HIS65 4.3 5.5 1.0
CU A:CU503 4.3 6.3 0.6
CU A:CU503 4.3 6.3 0.2
CU A:CU502 4.4 7.9 0.4
CB A:PHE450 4.4 6.6 1.0
HD21 A:LEU459 4.4 8.8 1.0
CD2 A:HIS65 4.5 6.4 1.0
HB2 A:PHE450 4.5 7.3 1.0
CG A:PHE450 4.5 6.1 1.0
NE2 A:HIS65 4.6 6.6 1.0
HE2 A:PHE450 4.6 7.9 1.0
CE2 A:PHE450 4.7 8.3 1.0
NE2 A:HIS400 4.7 6.6 1.0
HD1 A:HIS452 4.8 8.5 1.0
HD1 A:HIS402 4.8 7.3 1.0
HD1 A:HIS112 4.8 7.9 1.0
HD22 A:LEU459 4.9 8.8 1.0

Copper binding site 2 out of 7 in 6ri6

Go back to Copper Binding Sites List in 6ri6
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. Second Structure of the Series with 400 Kgy Dose.


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. Second Structure of the Series with 400 Kgy Dose. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu501

b:5.3
occ:0.40
CU A:CU501 0.0 5.3 0.4
CU A:CU501 0.8 8.2 0.6
O2 A:OXY512 1.8 9.1 0.2
O A:HOH601 1.8 8.4 0.5
O1 A:OXY512 1.9 8.6 0.2
NE2 A:HIS402 2.1 6.3 1.0
NE2 A:HIS112 2.2 7.4 1.0
O A:HOH608 2.2 5.1 0.4
NE2 A:HIS452 2.2 9.5 1.0
O A:HOH613 2.8 5.5 0.2
CE1 A:HIS402 3.0 6.4 1.0
CD2 A:HIS112 3.0 6.7 1.0
HD2 A:HIS400 3.0 5.2 1.0
CE1 A:HIS452 3.1 8.2 1.0
HD2 A:HIS112 3.1 7.9 1.0
HE1 A:HIS402 3.1 7.3 1.0
CD2 A:HIS402 3.1 6.1 1.0
HE1 A:HIS452 3.1 8.5 1.0
CE1 A:HIS112 3.2 8.0 1.0
HD2 A:HIS402 3.3 7.3 1.0
CD2 A:HIS452 3.4 8.7 1.0
HE1 A:HIS112 3.5 7.9 1.0
CU A:CU502 3.6 7.9 0.4
HD2 A:HIS65 3.6 5.5 1.0
HD2 A:HIS452 3.6 8.5 1.0
HE1 A:HIS110 3.6 8.7 1.0
O A:HOH614 3.7 12.2 0.8
CU A:CU503 3.8 6.3 0.6
CU A:CU503 3.8 6.3 0.2
CD2 A:HIS400 3.8 6.5 1.0
CD2 A:HIS65 3.8 6.4 1.0
HD2 A:PHE450 4.0 7.9 1.0
NE2 A:HIS65 4.0 6.6 1.0
ND1 A:HIS402 4.1 6.3 1.0
CG A:HIS402 4.2 6.0 1.0
CG A:HIS112 4.2 6.3 1.0
NE2 A:HIS400 4.2 6.6 1.0
HB3 A:PHE450 4.3 7.3 1.0
ND1 A:HIS452 4.3 7.5 1.0
ND1 A:HIS112 4.3 7.3 1.0
CU A:CU502 4.4 5.2 0.6
CE1 A:HIS110 4.4 6.6 1.0
CG A:HIS452 4.4 7.4 1.0
NE2 A:HIS454 4.4 6.2 1.0
HB3 A:PRO80 4.5 7.1 1.0
HD2 A:HIS454 4.5 5.8 1.0
CG A:HIS65 4.7 6.5 1.0
CD2 A:PHE450 4.7 7.0 1.0
CD2 A:HIS454 4.7 6.0 1.0
NE2 A:HIS110 4.7 6.7 1.0
HD21 A:LEU459 4.8 8.8 1.0
CE1 A:HIS65 4.8 6.5 1.0
HD1 A:HIS402 4.9 7.3 1.0
HD1 A:HIS452 5.0 8.5 1.0

Copper binding site 3 out of 7 in 6ri6

Go back to Copper Binding Sites List in 6ri6
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. Second Structure of the Series with 400 Kgy Dose.


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. Second Structure of the Series with 400 Kgy Dose. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu502

b:5.2
occ:0.55
CU A:CU502 0.0 5.2 0.6
CU A:CU502 0.9 7.9 0.4
ND1 A:HIS67 1.9 6.6 1.0
NE2 A:HIS110 2.0 6.7 1.0
NE2 A:HIS454 2.1 6.2 1.0
O A:HOH613 2.4 5.5 0.2
O2 A:OXY512 2.7 9.1 0.2
HB2 A:HIS67 2.7 5.8 1.0
O A:HOH608 2.9 5.1 0.4
CG A:HIS67 2.9 6.6 1.0
CE1 A:HIS67 2.9 6.3 1.0
CD2 A:HIS110 2.9 6.5 1.0
O A:HOH601 3.0 8.4 0.5
CE1 A:HIS110 3.0 6.6 1.0
CE1 A:HIS454 3.0 6.2 1.0
HD2 A:HIS110 3.1 8.6 1.0
HE1 A:HIS454 3.1 5.8 1.0
HE1 A:HIS67 3.1 5.8 1.0
HD2 A:HIS65 3.1 5.5 1.0
CD2 A:HIS454 3.3 6.0 1.0
HE1 A:HIS110 3.3 8.7 1.0
CB A:HIS67 3.3 6.5 1.0
HZ2 A:TRP108 3.5 7.6 1.0
HD2 A:HIS454 3.5 5.8 1.0
O1 A:OXY512 3.5 8.6 0.2
HB2 A:ALA244 3.6 7.6 1.0
CZ2 A:TRP108 3.7 6.4 1.0
HB3 A:HIS67 3.9 5.8 1.0
CD2 A:HIS65 3.9 6.4 1.0
HE1 A:TRP108 3.9 7.6 1.0
CE2 A:TRP108 4.0 6.0 1.0
NE2 A:HIS67 4.0 6.4 1.0
CU A:CU503 4.0 6.3 0.6
CU A:CU503 4.0 6.3 0.2
CD2 A:HIS67 4.0 6.7 1.0
NE1 A:TRP108 4.1 6.1 1.0
CG A:HIS110 4.1 6.0 1.0
ND1 A:HIS110 4.1 6.2 1.0
ND1 A:HIS454 4.2 6.0 1.0
HA A:HIS67 4.2 5.6 1.0
HD2 A:HIS400 4.3 5.2 1.0
CG A:HIS454 4.3 5.8 1.0
NE2 A:HIS65 4.3 6.6 1.0
HB1 A:ALA244 4.3 7.6 1.0
CB A:ALA244 4.4 6.1 1.0
CU A:CU501 4.4 5.3 0.4
CA A:HIS67 4.4 5.7 1.0
NE2 A:HIS400 4.4 6.6 1.0
CD2 A:HIS400 4.4 6.5 1.0
CH2 A:TRP108 4.5 6.4 1.0
O A:HOH614 4.6 12.2 0.8
HH2 A:TRP108 4.7 7.6 1.0
HE2 A:HIS67 4.8 5.8 1.0
HB3 A:ALA244 4.8 7.6 1.0
CD2 A:TRP108 4.8 5.9 1.0
HD1 A:HIS110 4.9 8.6 1.0
HD2 A:HIS67 4.9 5.8 1.0
HE1 A:HIS452 4.9 8.5 1.0
HD1 A:HIS454 4.9 5.8 1.0
CD1 A:TRP108 5.0 6.2 1.0

Copper binding site 4 out of 7 in 6ri6

Go back to Copper Binding Sites List in 6ri6
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. Second Structure of the Series with 400 Kgy Dose.


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. Second Structure of the Series with 400 Kgy Dose. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu502

b:7.9
occ:0.40
CU A:CU502 0.0 7.9 0.4
CU A:CU502 0.9 5.2 0.6
O2 A:OXY512 1.9 9.1 0.2
O A:HOH613 1.9 5.5 0.2
NE2 A:HIS454 1.9 6.2 1.0
O A:HOH608 2.2 5.1 0.4
O A:HOH601 2.2 8.4 0.5
ND1 A:HIS67 2.2 6.6 1.0
NE2 A:HIS110 2.3 6.7 1.0
O1 A:OXY512 2.8 8.6 0.2
CD2 A:HIS454 2.9 6.0 1.0
HD2 A:HIS65 2.9 5.5 1.0
CE1 A:HIS454 3.0 6.2 1.0
CE1 A:HIS110 3.0 6.6 1.0
HE1 A:HIS110 3.0 8.7 1.0
CE1 A:HIS67 3.1 6.3 1.0
HD2 A:HIS454 3.1 5.8 1.0
HE1 A:HIS67 3.1 5.8 1.0
HE1 A:HIS454 3.2 5.8 1.0
HB2 A:HIS67 3.3 5.8 1.0
CG A:HIS67 3.4 6.6 1.0
CD2 A:HIS110 3.5 6.5 1.0
HD2 A:HIS400 3.6 5.2 1.0
CU A:CU501 3.6 5.3 0.4
CU A:CU503 3.6 6.3 0.6
CU A:CU503 3.6 6.3 0.2
CD2 A:HIS65 3.7 6.4 1.0
HD2 A:HIS110 3.8 8.6 1.0
CD2 A:HIS400 3.8 6.5 1.0
CB A:HIS67 3.9 6.5 1.0
NE2 A:HIS400 3.9 6.6 1.0
HB2 A:ALA244 4.0 7.6 1.0
NE2 A:HIS65 4.1 6.6 1.0
CG A:HIS454 4.1 5.8 1.0
ND1 A:HIS454 4.1 6.0 1.0
O A:HOH614 4.1 12.2 0.8
HZ2 A:TRP108 4.1 7.6 1.0
HE1 A:HIS452 4.1 8.5 1.0
ND1 A:HIS110 4.2 6.2 1.0
NE2 A:HIS67 4.3 6.4 1.0
CU A:CU501 4.4 8.2 0.6
HA A:HIS67 4.4 5.6 1.0
CD2 A:HIS67 4.4 6.7 1.0
CZ2 A:TRP108 4.5 6.4 1.0
CG A:HIS110 4.5 6.0 1.0
HD2 A:HIS112 4.5 7.9 1.0
HB3 A:HIS67 4.6 5.8 1.0
HB1 A:ALA244 4.6 7.6 1.0
HE1 A:TRP108 4.7 7.6 1.0
CG A:HIS400 4.7 6.5 1.0
CB A:ALA244 4.7 6.1 1.0
CE1 A:HIS452 4.8 8.2 1.0
CA A:HIS67 4.8 5.7 1.0
CE2 A:TRP108 4.8 6.0 1.0
NE2 A:HIS452 4.8 9.5 1.0
CE1 A:HIS400 4.9 6.3 1.0
HD1 A:HIS454 4.9 5.8 1.0
NE1 A:TRP108 4.9 6.1 1.0
NE2 A:HIS112 4.9 7.4 1.0
HD1 A:HIS110 4.9 8.6 1.0
CG A:HIS65 4.9 6.5 1.0
NE2 A:HIS402 5.0 6.3 1.0
CD2 A:HIS112 5.0 6.7 1.0
HE2 A:HIS67 5.0 5.8 1.0

Copper binding site 5 out of 7 in 6ri6

Go back to Copper Binding Sites List in 6ri6
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. Second Structure of the Series with 400 Kgy Dose.


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. Second Structure of the Series with 400 Kgy Dose. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu503

b:6.3
occ:0.23
CU A:CU503 0.0 6.3 0.2
CU A:CU503 0.0 6.3 0.6
O A:HOH613 1.8 5.5 0.2
F A:F510 1.8 7.3 0.6
NE2 A:HIS65 1.9 6.6 1.0
NE2 A:HIS400 1.9 6.6 1.0
O A:HOH608 2.0 5.1 0.4
O A:HOH691 2.4 6.8 0.2
F A:F510 2.5 10.6 0.2
CE1 A:HIS65 2.9 6.5 1.0
CE1 A:HIS400 2.9 6.3 1.0
CD2 A:HIS400 2.9 6.5 1.0
CD2 A:HIS65 3.0 6.4 1.0
HA A:HIS67 3.0 5.6 1.0
HE1 A:HIS65 3.0 5.5 1.0
HD2 A:HIS400 3.1 5.2 1.0
HE1 A:HIS400 3.1 5.2 1.0
H A:GLY68 3.1 5.6 1.0
HD2 A:HIS65 3.2 5.5 1.0
CD2 A:HIS402 3.3 6.1 1.0
NE2 A:HIS402 3.4 6.3 1.0
HD2 A:HIS402 3.4 7.3 1.0
ND1 A:HIS67 3.5 6.6 1.0
O2 A:OXY512 3.6 9.1 0.2
CU A:CU502 3.6 7.9 0.4
HA A:HIS402 3.6 6.8 1.0
CG A:HIS402 3.6 6.0 1.0
CU A:CU501 3.8 5.3 0.4
CG A:HIS67 3.8 6.6 1.0
CE1 A:HIS402 3.8 6.4 1.0
CA A:HIS67 3.8 5.7 1.0
CE1 A:HIS67 3.9 6.3 1.0
N A:GLY68 4.0 5.7 1.0
ND1 A:HIS402 4.0 6.3 1.0
ND1 A:HIS65 4.0 6.6 1.0
CU A:CU502 4.0 5.2 0.6
ND1 A:HIS400 4.0 6.3 1.0
CG A:HIS400 4.1 6.5 1.0
CG A:HIS65 4.1 6.5 1.0
O A:HOH601 4.1 8.4 0.5
HB2 A:HIS67 4.1 5.8 1.0
CB A:HIS67 4.2 6.5 1.0
HE1 A:HIS67 4.2 5.8 1.0
HE1 A:HIS402 4.3 7.3 1.0
CD2 A:HIS67 4.3 6.7 1.0
CU A:CU501 4.3 8.2 0.6
CA A:HIS402 4.4 6.1 1.0
NE2 A:HIS67 4.4 6.4 1.0
C A:HIS67 4.4 5.8 1.0
CB A:HIS402 4.5 6.4 1.0
O A:HOH910 4.5 12.5 1.0
HD1 A:HIS402 4.5 7.3 1.0
O A:HOH984 4.7 11.3 1.0
HB3 A:HIS402 4.7 7.3 1.0
O1 A:OXY512 4.7 8.6 0.2
N A:HIS402 4.7 5.8 1.0
HD1 A:HIS65 4.8 5.5 1.0
HA2 A:GLY68 4.8 6.7 1.0
HD1 A:HIS400 4.8 5.2 1.0
HD2 A:HIS67 4.9 5.8 1.0
N A:HIS67 4.9 5.7 1.0
HE2 A:HIS67 4.9 5.8 1.0
HD2 A:HIS112 5.0 7.9 1.0
O A:LEU401 5.0 6.5 1.0
HD2 A:HIS454 5.0 5.8 1.0

Copper binding site 6 out of 7 in 6ri6

Go back to Copper Binding Sites List in 6ri6
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. Second Structure of the Series with 400 Kgy Dose.


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. Second Structure of the Series with 400 Kgy Dose. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu503

b:6.3
occ:0.60
CU A:CU503 0.0 6.3 0.6
CU A:CU503 0.0 6.3 0.2
O A:HOH613 1.8 5.5 0.2
F A:F510 1.8 7.3 0.6
NE2 A:HIS65 1.9 6.6 1.0
NE2 A:HIS400 1.9 6.6 1.0
O A:HOH608 2.0 5.1 0.4
O A:HOH691 2.4 6.8 0.2
F A:F510 2.5 10.6 0.2
CE1 A:HIS65 2.9 6.5 1.0
CE1 A:HIS400 2.9 6.3 1.0
CD2 A:HIS400 2.9 6.5 1.0
CD2 A:HIS65 3.0 6.4 1.0
HA A:HIS67 3.0 5.6 1.0
HE1 A:HIS65 3.0 5.5 1.0
HD2 A:HIS400 3.1 5.2 1.0
HE1 A:HIS400 3.1 5.2 1.0
H A:GLY68 3.1 5.6 1.0
HD2 A:HIS65 3.2 5.5 1.0
CD2 A:HIS402 3.3 6.1 1.0
NE2 A:HIS402 3.4 6.3 1.0
HD2 A:HIS402 3.4 7.3 1.0
ND1 A:HIS67 3.5 6.6 1.0
O2 A:OXY512 3.6 9.1 0.2
CU A:CU502 3.6 7.9 0.4
HA A:HIS402 3.6 6.8 1.0
CG A:HIS402 3.6 6.0 1.0
CU A:CU501 3.8 5.3 0.4
CG A:HIS67 3.8 6.6 1.0
CE1 A:HIS402 3.8 6.4 1.0
CA A:HIS67 3.8 5.7 1.0
CE1 A:HIS67 3.9 6.3 1.0
N A:GLY68 4.0 5.7 1.0
ND1 A:HIS402 4.0 6.3 1.0
ND1 A:HIS65 4.0 6.6 1.0
CU A:CU502 4.0 5.2 0.6
ND1 A:HIS400 4.0 6.3 1.0
CG A:HIS400 4.1 6.5 1.0
CG A:HIS65 4.1 6.5 1.0
O A:HOH601 4.1 8.4 0.5
HB2 A:HIS67 4.1 5.8 1.0
CB A:HIS67 4.2 6.5 1.0
HE1 A:HIS67 4.2 5.8 1.0
HE1 A:HIS402 4.3 7.3 1.0
CD2 A:HIS67 4.3 6.7 1.0
CU A:CU501 4.3 8.2 0.6
CA A:HIS402 4.4 6.1 1.0
NE2 A:HIS67 4.4 6.4 1.0
C A:HIS67 4.4 5.8 1.0
CB A:HIS402 4.5 6.4 1.0
O A:HOH910 4.5 12.5 1.0
HD1 A:HIS402 4.5 7.3 1.0
O A:HOH984 4.7 11.3 1.0
HB3 A:HIS402 4.7 7.3 1.0
O1 A:OXY512 4.7 8.6 0.2
N A:HIS402 4.7 5.8 1.0
HD1 A:HIS65 4.8 5.5 1.0
HA2 A:GLY68 4.8 6.7 1.0
HD1 A:HIS400 4.8 5.2 1.0
HD2 A:HIS67 4.9 5.8 1.0
N A:HIS67 4.9 5.7 1.0
HE2 A:HIS67 4.9 5.8 1.0
HD2 A:HIS112 5.0 7.9 1.0
O A:LEU401 5.0 6.5 1.0
HD2 A:HIS454 5.0 5.8 1.0

Copper binding site 7 out of 7 in 6ri6

Go back to Copper Binding Sites List in 6ri6
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. Second Structure of the Series with 400 Kgy Dose.


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. Second Structure of the Series with 400 Kgy Dose. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu504

b:5.9
occ:0.85
ND1 A:HIS458 2.0 6.9 1.0
ND1 A:HIS397 2.0 6.9 1.0
SG A:CYS453 2.2 6.8 1.0
HD11 A:ILE455 2.6 7.5 1.0
HB A:ILE455 2.9 7.5 1.0
CE1 A:HIS397 2.9 7.3 1.0
CE1 A:HIS458 3.0 7.2 1.0
HD2 A:PHE463 3.0 10.6 1.0
CG A:HIS458 3.0 6.9 1.0
HB2 A:HIS458 3.1 7.5 1.0
HB3 A:HIS397 3.1 10.1 1.0
HE1 A:HIS397 3.1 7.3 1.0
CG A:HIS397 3.1 6.8 1.0
HE1 A:HIS458 3.2 7.3 1.0
HB3 A:HIS458 3.3 7.5 1.0
CB A:CYS453 3.3 6.6 1.0
CB A:HIS458 3.3 6.8 1.0
HA A:HIS397 3.4 7.5 1.0
HB2 A:CYS453 3.4 6.5 1.0
HB3 A:CYS453 3.4 6.5 1.0
CB A:HIS397 3.5 6.7 1.0
HE2 A:PHE463 3.5 10.6 1.0
CD1 A:ILE455 3.6 7.1 1.0
HD2 A:PRO398 3.8 7.5 1.0
CD2 A:PHE463 3.8 6.8 1.0
CB A:ILE455 3.8 6.5 1.0
H A:ILE455 3.9 7.5 1.0
CA A:HIS397 4.0 6.7 1.0
HD12 A:ILE455 4.0 7.5 1.0
CE2 A:PHE463 4.0 7.2 1.0
CG1 A:ILE455 4.1 6.9 1.0
NE2 A:HIS397 4.1 7.7 1.0
HG13 A:ILE455 4.1 7.5 1.0
NE2 A:HIS458 4.1 7.7 1.0
HD13 A:ILE455 4.1 7.5 1.0
CD2 A:HIS458 4.2 7.2 1.0
CD2 A:HIS397 4.2 7.6 1.0
HB2 A:HIS397 4.4 10.1 1.0
HG21 A:ILE455 4.5 7.5 1.0
HG22 A:ILE455 4.6 7.5 1.0
CG2 A:ILE455 4.6 6.8 1.0
HZ A:PHE341 4.6 10.1 1.0
CD A:PRO398 4.6 6.6 1.0
CA A:CYS453 4.7 6.2 1.0
O A:GLY394 4.7 10.1 1.0
N A:ILE455 4.7 6.3 1.0
CZ A:PHE341 4.8 8.8 1.0
HE2 A:PHE341 4.8 10.1 1.0
CA A:ILE455 4.8 6.5 1.0
HE1 A:PHE399 4.8 10.2 1.0
HD3 A:PRO398 4.8 7.5 1.0
HA A:CYS453 4.8 5.9 1.0
HE2 A:HIS397 4.9 7.3 1.0
HA2 A:GLY395 4.9 9.6 1.0
CE2 A:PHE341 4.9 8.6 1.0
CA A:HIS458 4.9 7.0 1.0
HE2 A:HIS458 4.9 7.3 1.0
O A:ILE455 4.9 6.8 1.0
C A:HIS397 5.0 6.2 1.0
HB3 A:PHE463 5.0 7.6 1.0
N A:HIS397 5.0 7.1 1.0
HG12 A:ILE455 5.0 7.5 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 11:25:36 2020

Last articles

Zn in 8WB0
Zn in 8WAX
Zn in 8WAU
Zn in 8WAZ
Zn in 8WAY
Zn in 8WAV
Zn in 8WAW
Zn in 8WAT
Zn in 8W7M
Zn in 8WD3
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy