Atomistry » Copper » PDB 5lww-5nlo » 5mid
Atomistry »
  Copper »
    PDB 5lww-5nlo »
      5mid »

Copper in PDB 5mid: The Study of the X-Ray Induced Enzymatic Reduction of Molecular Oxygen to Water For Laccase From Steccherinum Murashkinskyi.the 14-Th Structure of the Series with Total Exposition Time 393 Min.

Enzymatic activity of The Study of the X-Ray Induced Enzymatic Reduction of Molecular Oxygen to Water For Laccase From Steccherinum Murashkinskyi.the 14-Th Structure of the Series with Total Exposition Time 393 Min.

All present enzymatic activity of The Study of the X-Ray Induced Enzymatic Reduction of Molecular Oxygen to Water For Laccase From Steccherinum Murashkinskyi.the 14-Th Structure of the Series with Total Exposition Time 393 Min.:
1.10.3.2;

Protein crystallography data

The structure of The Study of the X-Ray Induced Enzymatic Reduction of Molecular Oxygen to Water For Laccase From Steccherinum Murashkinskyi.the 14-Th Structure of the Series with Total Exposition Time 393 Min., PDB code: 5mid 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) 67.50 / 1.35
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 56.370, 84.390, 112.480, 90.00, 90.00, 90.00
R / Rfree (%) 13.2 / 15

Other elements in 5mid:

The structure of The Study of the X-Ray Induced Enzymatic Reduction of Molecular Oxygen to Water For Laccase From Steccherinum Murashkinskyi.the 14-Th Structure of the Series with Total Exposition Time 393 Min. also contains other interesting chemical elements:

Sodium (Na) 1 atom

Copper Binding Sites:

The binding sites of Copper atom in the The Study of the X-Ray Induced Enzymatic Reduction of Molecular Oxygen to Water For Laccase From Steccherinum Murashkinskyi.the 14-Th Structure of the Series with Total Exposition Time 393 Min. (pdb code 5mid). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 6 binding sites of Copper where determined in the The Study of the X-Ray Induced Enzymatic Reduction of Molecular Oxygen to Water For Laccase From Steccherinum Murashkinskyi.the 14-Th Structure of the Series with Total Exposition Time 393 Min., PDB code: 5mid:
Jump to Copper binding site number: 1; 2; 3; 4; 5; 6;

Copper binding site 1 out of 6 in 5mid

Go back to Copper Binding Sites List in 5mid
Copper binding site 1 out of 6 in the The Study of the X-Ray Induced Enzymatic Reduction of Molecular Oxygen to Water For Laccase From Steccherinum Murashkinskyi.the 14-Th Structure of the Series with Total Exposition Time 393 Min.


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of The Study of the X-Ray Induced Enzymatic Reduction of Molecular Oxygen to Water For Laccase From Steccherinum Murashkinskyi.the 14-Th Structure of the Series with Total Exposition Time 393 Min. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu601

b:6.2
occ:0.20
 CU A:CU601 0.0 6.2 0.2
CU A:CU601 0.7 6.8 0.7
O A:HOH704 1.7 7.9 0.5
O A:HOH702 1.8 8.9 0.2
O2 A:OXY609 2.0 3.8 0.2
NE2 A:HIS402 2.1 6.3 1.0
O1 A:OXY609 2.1 3.6 0.2
NE2 A:HIS452 2.2 8.1 1.0
NE2 A:HIS112 2.2 6.8 1.0
O A:HOH705 2.5 5.2 0.2
CE1 A:HIS402 3.0 6.2 1.0
HD2 A:HIS400 3.0 6.2 1.0
CE1 A:HIS452 3.0 8.7 1.0
CD2 A:HIS112 3.1 6.7 1.0
HE1 A:HIS402 3.1 6.2 1.0
HE1 A:HIS452 3.1 8.2 1.0
HD2 A:HIS112 3.1 6.7 1.0
CD2 A:HIS402 3.2 6.2 1.0
CE1 A:HIS112 3.3 7.4 1.0
CD2 A:HIS452 3.3 7.4 1.0
HD2 A:HIS402 3.4 6.2 1.0
HE1 A:HIS112 3.5 7.2 1.0
O A:HOH701 3.6 10.8 0.5
HD2 A:HIS452 3.6 7.5 1.0
CD2 A:HIS400 3.8 6.3 1.0
HD2 A:PHE450 3.9 8.1 1.0
HE1 A:HIS110 3.9 6.5 1.0
CU A:CU603 3.9 6.5 0.8
HD2 A:HIS65 3.9 6.3 1.0
O1 A:OXY610 4.1 17.9 0.5
CD2 A:HIS65 4.1 6.3 1.0
ND1 A:HIS402 4.1 6.2 1.0
CU A:CU602 4.1 6.1 0.2
HB3 A:PHE450 4.1 6.8 1.0
NE2 A:HIS65 4.2 6.6 1.0
ND1 A:HIS452 4.2 7.4 1.0
CG A:HIS402 4.2 6.0 1.0
CG A:HIS112 4.3 6.7 1.0
NE2 A:HIS400 4.3 6.4 1.0
ND1 A:HIS112 4.3 7.1 1.0
CG A:HIS452 4.4 7.0 1.0
HB3 A:PRO80 4.4 6.2 1.0
CD2 A:PHE450 4.6 8.2 1.0
HD2 A:HIS454 4.6 6.8 1.0
CU A:CU602 4.7 5.9 0.7
NE2 A:HIS454 4.7 7.1 1.0
CE1 A:HIS110 4.7 6.7 1.0
HD21 A:LEU459 4.7 8.6 1.0
O2 A:OXY610 4.8 17.2 0.5
CD2 A:HIS454 4.8 6.8 1.0
CG A:HIS65 4.8 6.1 1.0
HD1 A:HIS402 4.9 6.1 1.0
CE1 A:HIS65 4.9 6.2 1.0
CB A:PHE450 5.0 6.9 1.0
HD1 A:HIS452 5.0 7.6 1.0

Copper binding site 2 out of 6 in 5mid

Go back to Copper Binding Sites List in 5mid
Copper binding site 2 out of 6 in the The Study of the X-Ray Induced Enzymatic Reduction of Molecular Oxygen to Water For Laccase From Steccherinum Murashkinskyi.the 14-Th Structure of the Series with Total Exposition Time 393 Min.


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of The Study of the X-Ray Induced Enzymatic Reduction of Molecular Oxygen to Water For Laccase From Steccherinum Murashkinskyi.the 14-Th Structure of the Series with Total Exposition Time 393 Min. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu601

b:6.8
occ:0.70
 CU A:CU601 0.0 6.8 0.7
CU A:CU601 0.7 6.2 0.2
NE2 A:HIS452 1.9 8.1 1.0
NE2 A:HIS402 2.0 6.3 1.0
NE2 A:HIS112 2.0 6.8 1.0
O A:HOH704 2.4 7.9 0.5
O A:HOH702 2.4 8.9 0.2
O2 A:OXY609 2.5 3.8 0.2
O1 A:OXY609 2.8 3.6 0.2
CE1 A:HIS402 2.9 6.2 1.0
CD2 A:HIS452 2.9 7.4 1.0
CE1 A:HIS112 3.0 7.4 1.0
CE1 A:HIS452 3.0 8.7 1.0
HE1 A:HIS402 3.0 6.2 1.0
HD2 A:HIS452 3.1 7.5 1.0
CD2 A:HIS402 3.1 6.2 1.0
HE1 A:HIS112 3.1 7.2 1.0
CD2 A:HIS112 3.1 6.7 1.0
O A:HOH705 3.1 5.2 0.2
HE1 A:HIS452 3.2 8.2 1.0
HD2 A:PHE450 3.3 8.1 1.0
HD2 A:HIS402 3.3 6.2 1.0
HD2 A:HIS400 3.3 6.2 1.0
HD2 A:HIS112 3.3 6.7 1.0
HB3 A:PHE450 3.6 6.8 1.0
O A:HOH701 3.8 10.8 0.5
CD2 A:PHE450 3.9 8.2 1.0
ND1 A:HIS402 4.0 6.2 1.0
HB3 A:PRO80 4.0 6.2 1.0
ND1 A:HIS452 4.1 7.4 1.0
CG A:HIS452 4.1 7.0 1.0
ND1 A:HIS112 4.1 7.1 1.0
CG A:HIS402 4.2 6.0 1.0
CD2 A:HIS400 4.2 6.3 1.0
CG A:HIS112 4.2 6.7 1.0
O1 A:OXY610 4.3 17.9 0.5
HE1 A:HIS110 4.4 6.5 1.0
CU A:CU603 4.4 6.5 0.8
CB A:PHE450 4.4 6.9 1.0
HD21 A:LEU459 4.4 8.6 1.0
HD2 A:HIS65 4.5 6.3 1.0
HB2 A:PHE450 4.5 6.8 1.0
CD2 A:HIS65 4.6 6.3 1.0
CG A:PHE450 4.6 7.0 1.0
NE2 A:HIS65 4.6 6.6 1.0
HE2 A:PHE450 4.7 8.7 1.0
CE2 A:PHE450 4.8 8.8 1.0
NE2 A:HIS400 4.8 6.4 1.0
CU A:CU602 4.8 6.1 0.2
HD1 A:HIS402 4.8 6.1 1.0
HD1 A:HIS452 4.9 7.6 1.0
O2 A:OXY610 4.9 17.2 0.5
HD1 A:HIS112 4.9 7.0 1.0
HD22 A:LEU459 5.0 8.6 1.0
CB A:PRO80 5.0 6.2 1.0

Copper binding site 3 out of 6 in 5mid

Go back to Copper Binding Sites List in 5mid
Copper binding site 3 out of 6 in the The Study of the X-Ray Induced Enzymatic Reduction of Molecular Oxygen to Water For Laccase From Steccherinum Murashkinskyi.the 14-Th Structure of the Series with Total Exposition Time 393 Min.


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 3 of The Study of the X-Ray Induced Enzymatic Reduction of Molecular Oxygen to Water For Laccase From Steccherinum Murashkinskyi.the 14-Th Structure of the Series with Total Exposition Time 393 Min. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu602

b:6.1
occ:0.20
 CU A:CU602 0.0 6.1 0.2
CU A:CU602 0.6 5.9 0.7
O1 A:OXY609 2.0 3.6 0.2
NE2 A:HIS454 2.0 7.1 1.0
NE2 A:HIS110 2.1 6.6 1.0
ND1 A:HIS67 2.1 6.3 1.0
O A:HOH705 2.3 5.2 0.2
O A:HOH702 2.4 8.9 0.2
O A:HOH704 2.4 7.9 0.5
O2 A:OXY609 2.7 3.8 0.2
HD2 A:HIS65 2.8 6.3 1.0
CE1 A:HIS110 2.9 6.7 1.0
HE1 A:HIS110 3.0 6.5 1.0
HB2 A:HIS67 3.0 5.7 1.0
CE1 A:HIS454 3.0 7.5 1.0
CE1 A:HIS67 3.1 6.2 1.0
CD2 A:HIS454 3.1 6.8 1.0
HE1 A:HIS67 3.2 6.2 1.0
HE1 A:HIS454 3.2 7.2 1.0
HD2 A:HIS454 3.2 6.8 1.0
CG A:HIS67 3.2 5.8 1.0
CD2 A:HIS110 3.3 6.0 1.0
HD2 A:HIS110 3.5 6.2 1.0
CD2 A:HIS65 3.6 6.3 1.0
CB A:HIS67 3.6 5.7 1.0
CU A:CU603 3.7 6.5 0.8
HD2 A:HIS400 3.9 6.2 1.0
HZ2 A:TRP108 3.9 6.0 1.0
HB2 A:ALA244 4.0 5.4 1.0
O A:HOH701 4.1 10.8 0.5
NE2 A:HIS65 4.1 6.6 1.0
CD2 A:HIS400 4.1 6.3 1.0
ND1 A:HIS110 4.1 6.3 1.0
CU A:CU601 4.1 6.2 0.2
NE2 A:HIS400 4.1 6.4 1.0
ND1 A:HIS454 4.2 7.0 1.0
CG A:HIS454 4.2 6.6 1.0
NE2 A:HIS67 4.2 6.2 1.0
CZ2 A:TRP108 4.2 6.1 1.0
HB3 A:HIS67 4.3 5.7 1.0
CG A:HIS110 4.3 6.1 1.0
CD2 A:HIS67 4.3 6.6 1.0
HA A:HIS67 4.3 5.7 1.0
HE1 A:TRP108 4.5 6.1 1.0
CE2 A:TRP108 4.5 5.8 1.0
HD2 A:HIS112 4.6 6.7 1.0
HB1 A:ALA244 4.6 5.4 1.0
HE1 A:HIS452 4.6 8.2 1.0
NE1 A:TRP108 4.6 6.0 1.0
CA A:HIS67 4.6 5.7 1.0
CB A:ALA244 4.7 5.5 1.0
O1 A:OXY610 4.7 17.9 0.5
CU A:CU601 4.8 6.8 0.7
HD1 A:HIS110 4.8 6.3 1.0
CG A:HIS65 4.8 6.1 1.0
CH2 A:TRP108 4.9 6.3 1.0
HD1 A:HIS454 4.9 7.0 1.0
CG A:HIS400 5.0 5.8 1.0
HE2 A:HIS67 5.0 6.3 1.0
HB3 A:HIS65 5.0 6.2 1.0

Copper binding site 4 out of 6 in 5mid

Go back to Copper Binding Sites List in 5mid
Copper binding site 4 out of 6 in the The Study of the X-Ray Induced Enzymatic Reduction of Molecular Oxygen to Water For Laccase From Steccherinum Murashkinskyi.the 14-Th Structure of the Series with Total Exposition Time 393 Min.


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 4 of The Study of the X-Ray Induced Enzymatic Reduction of Molecular Oxygen to Water For Laccase From Steccherinum Murashkinskyi.the 14-Th Structure of the Series with Total Exposition Time 393 Min. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu602

b:5.9
occ:0.70
 CU A:CU602 0.0 5.9 0.7
CU A:CU602 0.6 6.1 0.2
ND1 A:HIS67 1.9 6.3 1.0
NE2 A:HIS110 2.0 6.6 1.0
NE2 A:HIS454 2.1 7.1 1.0
O1 A:OXY609 2.5 3.6 0.2
HB2 A:HIS67 2.8 5.7 1.0
O A:HOH705 2.8 5.2 0.2
O A:HOH702 2.9 8.9 0.2
CE1 A:HIS67 2.9 6.2 1.0
O A:HOH704 2.9 7.9 0.5
CG A:HIS67 3.0 5.8 1.0
CE1 A:HIS454 3.0 7.5 1.0
CD2 A:HIS110 3.0 6.0 1.0
CE1 A:HIS110 3.0 6.7 1.0
HD2 A:HIS65 3.1 6.3 1.0
HE1 A:HIS67 3.1 6.2 1.0
HE1 A:HIS454 3.1 7.2 1.0
HD2 A:HIS110 3.2 6.2 1.0
CD2 A:HIS454 3.2 6.8 1.0
O2 A:OXY609 3.2 3.8 0.2
HE1 A:HIS110 3.2 6.5 1.0
CB A:HIS67 3.4 5.7 1.0
HD2 A:HIS454 3.4 6.8 1.0
HZ2 A:TRP108 3.5 6.0 1.0
HB2 A:ALA244 3.6 5.4 1.0
CZ2 A:TRP108 3.7 6.1 1.0
CD2 A:HIS65 3.9 6.3 1.0
HB3 A:HIS67 3.9 5.7 1.0
HE1 A:TRP108 3.9 6.1 1.0
CE2 A:TRP108 4.0 5.8 1.0
NE2 A:HIS67 4.0 6.2 1.0
CU A:CU603 4.1 6.5 0.8
CD2 A:HIS67 4.1 6.6 1.0
NE1 A:TRP108 4.1 6.0 1.0
ND1 A:HIS110 4.1 6.3 1.0
CG A:HIS110 4.1 6.1 1.0
ND1 A:HIS454 4.2 7.0 1.0
CG A:HIS454 4.3 6.6 1.0
HD2 A:HIS400 4.3 6.2 1.0
HA A:HIS67 4.3 5.7 1.0
HB1 A:ALA244 4.4 5.4 1.0
NE2 A:HIS65 4.4 6.6 1.0
CB A:ALA244 4.4 5.5 1.0
O A:HOH701 4.4 10.8 0.5
NE2 A:HIS400 4.4 6.4 1.0
CD2 A:HIS400 4.4 6.3 1.0
CA A:HIS67 4.5 5.7 1.0
CH2 A:TRP108 4.5 6.3 1.0
CU A:CU601 4.7 6.2 0.2
HH2 A:TRP108 4.7 6.3 1.0
HE2 A:HIS67 4.8 6.3 1.0
HB3 A:ALA244 4.8 5.4 1.0
CD2 A:TRP108 4.9 5.8 1.0
HD1 A:HIS110 4.9 6.3 1.0
HD1 A:HIS454 4.9 7.0 1.0
HD2 A:HIS67 4.9 6.3 1.0
HD2 A:HIS112 5.0 6.7 1.0

Copper binding site 5 out of 6 in 5mid

Go back to Copper Binding Sites List in 5mid
Copper binding site 5 out of 6 in the The Study of the X-Ray Induced Enzymatic Reduction of Molecular Oxygen to Water For Laccase From Steccherinum Murashkinskyi.the 14-Th Structure of the Series with Total Exposition Time 393 Min.


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 5 of The Study of the X-Ray Induced Enzymatic Reduction of Molecular Oxygen to Water For Laccase From Steccherinum Murashkinskyi.the 14-Th Structure of the Series with Total Exposition Time 393 Min. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu603

b:6.5
occ:0.80
 NE2 A:HIS65 1.9 6.6 1.0
NE2 A:HIS400 1.9 6.4 1.0
O A:HOH705 2.0 5.2 0.2
O A:HOH955 2.0 2.7 0.2
O A:HOH1103 2.8 6.1 0.8
CE1 A:HIS65 2.8 6.2 1.0
CD2 A:HIS400 2.8 6.3 1.0
CD2 A:HIS65 2.9 6.3 1.0
CE1 A:HIS400 2.9 6.2 1.0
HE1 A:HIS65 3.0 6.2 1.0
HD2 A:HIS400 3.0 6.2 1.0
HA A:HIS67 3.1 5.7 1.0
HD2 A:HIS65 3.1 6.3 1.0
O1 A:OXY609 3.1 3.6 0.2
HE1 A:HIS400 3.1 6.1 1.0
O A:HOH704 3.3 7.9 0.5
H A:GLY68 3.3 5.7 1.0
O A:HOH702 3.4 8.9 0.2
CD2 A:HIS402 3.4 6.2 1.0
NE2 A:HIS402 3.5 6.3 1.0
ND1 A:HIS67 3.5 6.3 1.0
HD2 A:HIS402 3.6 6.2 1.0
CU A:CU602 3.7 6.1 0.2
HA A:HIS402 3.7 6.0 1.0
CG A:HIS402 3.8 6.0 1.0
CE1 A:HIS402 3.8 6.2 1.0
CG A:HIS67 3.8 5.8 1.0
CU A:CU601 3.9 6.2 0.2
CE1 A:HIS67 3.9 6.2 1.0
ND1 A:HIS65 4.0 6.0 1.0
ND1 A:HIS402 4.0 6.2 1.0
CA A:HIS67 4.0 5.7 1.0
ND1 A:HIS400 4.0 5.7 1.0
CG A:HIS400 4.0 5.8 1.0
CG A:HIS65 4.0 6.1 1.0
CU A:CU602 4.1 5.9 0.7
N A:GLY68 4.1 5.5 1.0
HB2 A:HIS67 4.1 5.7 1.0
HE1 A:HIS67 4.2 6.2 1.0
CB A:HIS67 4.2 5.7 1.0
HE1 A:HIS402 4.3 6.2 1.0
O2 A:OXY609 4.3 3.8 0.2
CU A:CU601 4.4 6.8 0.7
CD2 A:HIS67 4.4 6.6 1.0
NE2 A:HIS67 4.4 6.2 1.0
HD1 A:HIS402 4.5 6.1 1.0
CA A:HIS402 4.5 6.0 1.0
C A:HIS67 4.6 5.7 1.0
CB A:HIS402 4.6 6.1 1.0
O A:HOH967 4.7 9.6 1.0
HD1 A:HIS65 4.7 6.1 1.0
HD1 A:HIS400 4.8 5.8 1.0
HB3 A:HIS402 4.8 6.1 1.0
O A:HOH804 4.8 9.6 1.0
N A:HIS402 4.9 6.0 1.0
HD2 A:HIS454 4.9 6.8 1.0
HA2 A:GLY68 4.9 5.9 1.0
HD2 A:HIS112 4.9 6.7 1.0
HD2 A:HIS67 5.0 6.3 1.0
HE2 A:HIS67 5.0 6.3 1.0
O A:LEU401 5.0 6.3 1.0

Copper binding site 6 out of 6 in 5mid

Go back to Copper Binding Sites List in 5mid
Copper binding site 6 out of 6 in the The Study of the X-Ray Induced Enzymatic Reduction of Molecular Oxygen to Water For Laccase From Steccherinum Murashkinskyi.the 14-Th Structure of the Series with Total Exposition Time 393 Min.


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 6 of The Study of the X-Ray Induced Enzymatic Reduction of Molecular Oxygen to Water For Laccase From Steccherinum Murashkinskyi.the 14-Th Structure of the Series with Total Exposition Time 393 Min. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu604

b:6.1
occ:0.90
 ND1 A:HIS458 2.0 6.8 1.0
ND1 A:HIS397 2.0 6.9 1.0
SG A:CYS453 2.2 6.8 1.0
HD11 A:ILE455 2.7 6.0 1.0
CE1 A:HIS397 3.0 6.9 1.0
CE1 A:HIS458 3.0 7.4 1.0
HB A:ILE455 3.0 6.4 1.0
HD2 A:PHE463 3.1 6.5 1.0
CG A:HIS458 3.1 6.9 1.0
HE1 A:HIS397 3.1 7.0 1.0
HB3 A:HIS397 3.1 6.6 1.0
CG A:HIS397 3.1 6.3 1.0
HB2 A:HIS458 3.1 7.0 1.0
HE1 A:HIS458 3.2 7.2 1.0
HB3 A:HIS458 3.3 7.0 1.0
CB A:CYS453 3.3 6.4 1.0
HB2 A:CYS453 3.4 6.5 1.0
CB A:HIS458 3.4 7.0 1.0
HA A:HIS397 3.4 6.6 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 6.6 1.0
CD1 A:ILE455 3.6 5.8 1.0
HD2 A:PRO398 3.8 6.1 1.0
CD2 A:PHE463 3.8 6.3 1.0
CB A:ILE455 3.9 6.3 1.0
H A:ILE455 3.9 7.0 1.0
HD12 A:ILE455 3.9 6.0 1.0
CA A:HIS397 4.0 6.7 1.0
CG1 A:ILE455 4.1 6.3 1.0
HG13 A:ILE455 4.1 6.2 1.0
CE2 A:PHE463 4.1 6.8 1.0
NE2 A:HIS397 4.1 7.3 1.0
NE2 A:HIS458 4.1 7.4 1.0
CD2 A:HIS458 4.2 6.9 1.0
CD2 A:HIS397 4.2 7.1 1.0
HD13 A:ILE455 4.2 6.0 1.0
HB2 A:HIS397 4.4 6.6 1.0
HG21 A:ILE455 4.5 6.5 1.0
O A:GLY394 4.6 9.2 1.0
HG22 A:ILE455 4.6 6.5 1.0
HZ A:PHE341 4.6 7.8 1.0
CD A:PRO398 4.6 6.0 1.0
CG2 A:ILE455 4.6 6.7 1.0
CA A:CYS453 4.7 6.2 1.0
CZ A:PHE341 4.8 7.9 1.0
N A:ILE455 4.8 6.9 1.0
HD3 A:PRO398 4.8 6.1 1.0
HE2 A:PHE341 4.8 7.6 1.0
HE1 A:PHE399 4.9 7.9 1.0
HA A:CYS453 4.9 6.2 1.0
HE2 A:HIS397 4.9 7.2 1.0
CA A:HIS458 4.9 7.2 1.0
CE2 A:PHE341 4.9 7.3 1.0
CA A:ILE455 4.9 6.8 1.0
HE2 A:HIS458 4.9 7.3 1.0
C A:HIS397 5.0 6.3 1.0
N A:HIS397 5.0 6.6 1.0
O A:ILE455 5.0 7.0 1.0
HB3 A:PHE463 5.0 6.7 1.0
HG12 A:ILE455 5.0 6.2 1.0

Reference:

K.M.Polyakov, S.Gavryushov, S.Ivanova, T.V.Fedorova, O.A.Glazunova, A.N.Popov, O.V.Koroleva. Structural Study of the X-Ray-Induced Enzymatic Reduction of Molecular Oxygen to Water By Steccherinum Murashkinskyi Laccase: Insights Into the Reaction Mechanism. Acta Crystallogr D Struct V. 73 388 2017BIOL.
ISSN: ISSN 2059-7983
PubMed: 28471364
DOI: 10.1107/S2059798317003667
Page generated: Wed Jul 31 04:36:15 2024

Last articles

Zn in 9JYW
Zn in 9IR4
Zn in 9IR3
Zn in 9GMX
Zn in 9GMW
Zn in 9JEJ
Zn in 9ERF
Zn in 9ERE
Zn in 9EGV
Zn in 9EGW
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy