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Copper in PDB 5mi2: The Study of the X-Ray Induced Enzymatic Reduction of Molecular Oxygen to Water For Laccase From Steccherinum Murashkinskyi.the 10-Th Structure of the Series with Total Exposition Time 273 Min.

Enzymatic activity of The Study of the X-Ray Induced Enzymatic Reduction of Molecular Oxygen to Water For Laccase From Steccherinum Murashkinskyi.the 10-Th Structure of the Series with Total Exposition Time 273 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 10-Th Structure of the Series with Total Exposition Time 273 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 10-Th Structure of the Series with Total Exposition Time 273 Min., PDB code: 5mi2 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) 67.52 / 1.35
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 56.380, 84.410, 112.510, 90.00, 90.00, 90.00
R / Rfree (%) 13.1 / 14.8

Other elements in 5mi2:

The structure of The Study of the X-Ray Induced Enzymatic Reduction of Molecular Oxygen to Water For Laccase From Steccherinum Murashkinskyi.the 10-Th Structure of the Series with Total Exposition Time 273 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 10-Th Structure of the Series with Total Exposition Time 273 Min. (pdb code 5mi2). 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 10-Th Structure of the Series with Total Exposition Time 273 Min., PDB code: 5mi2:
Jump to Copper binding site number: 1; 2; 3; 4; 5; 6;

Copper binding site 1 out of 6 in 5mi2

Go back to Copper Binding Sites List in 5mi2
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 10-Th Structure of the Series with Total Exposition Time 273 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 10-Th Structure of the Series with Total Exposition Time 273 Min. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu601

b:8.0
occ:0.40
 CU A:CU601 0.0 8.0 0.4
CU A:CU601 0.7 5.5 0.5
O A:HOH704 1.7 4.7 0.3
O2 A:OXY609 2.0 7.5 0.3
NE2 A:HIS402 2.0 6.3 1.0
O1 A:OXY609 2.1 6.2 0.3
NE2 A:HIS452 2.1 8.7 1.0
O A:HOH701 2.1 7.7 0.3
NE2 A:HIS112 2.1 7.0 1.0
O A:HOH705 2.7 11.9 0.3
CE1 A:HIS402 2.9 6.1 1.0
CE1 A:HIS452 3.0 8.8 1.0
HE1 A:HIS402 3.0 6.1 1.0
CD2 A:HIS112 3.0 6.8 1.0
HD2 A:HIS400 3.1 6.2 1.0
HE1 A:HIS452 3.1 8.5 1.0
HD2 A:HIS112 3.1 6.8 1.0
CD2 A:HIS402 3.1 5.8 1.0
CE1 A:HIS112 3.2 7.4 1.0
CD2 A:HIS452 3.3 8.0 1.0
HD2 A:HIS402 3.4 5.9 1.0
HE1 A:HIS112 3.5 7.1 1.0
HD2 A:HIS452 3.5 8.0 1.0
O A:HOH702 3.6 10.0 0.5
HD2 A:PHE450 3.8 7.7 1.0
CD2 A:HIS400 3.9 6.3 1.0
HE1 A:HIS110 3.9 6.2 1.0
CU A:CU603 3.9 6.4 0.8
HD2 A:HIS65 4.0 6.4 1.0
HB3 A:PHE450 4.1 6.7 1.0
ND1 A:HIS402 4.1 6.2 1.0
O1 A:OXY610 4.1 15.3 0.5
CD2 A:HIS65 4.1 6.2 1.0
ND1 A:HIS452 4.2 7.7 1.0
CG A:HIS402 4.2 5.9 1.0
NE2 A:HIS65 4.2 6.5 1.0
CG A:HIS112 4.3 6.5 1.0
CU A:CU602 4.3 12.3 0.4
ND1 A:HIS112 4.3 6.7 1.0
CG A:HIS452 4.3 7.4 1.0
NE2 A:HIS400 4.4 6.1 1.0
HB3 A:PRO80 4.4 6.2 1.0
CD2 A:PHE450 4.5 7.8 1.0
HD2 A:HIS454 4.6 6.4 1.0
HD21 A:LEU459 4.7 8.0 1.0
CU A:CU602 4.7 4.2 0.5
NE2 A:HIS454 4.7 6.8 1.0
CE1 A:HIS110 4.8 6.4 1.0
O2 A:OXY610 4.8 15.4 0.5
CD2 A:HIS454 4.8 6.4 1.0
HD1 A:HIS402 4.8 6.1 1.0
CG A:HIS65 4.9 6.4 1.0
CB A:PHE450 4.9 6.8 1.0
HD1 A:HIS452 4.9 7.9 1.0
CE1 A:HIS65 5.0 6.5 1.0

Copper binding site 2 out of 6 in 5mi2

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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 10-Th Structure of the Series with Total Exposition Time 273 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 10-Th Structure of the Series with Total Exposition Time 273 Min. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu601

b:5.5
occ:0.50
 CU A:CU601 0.0 5.5 0.5
CU A:CU601 0.7 8.0 0.4
NE2 A:HIS452 1.9 8.7 1.0
NE2 A:HIS402 2.0 6.3 1.0
NE2 A:HIS112 2.0 7.0 1.0
O A:HOH704 2.3 4.7 0.3
O2 A:OXY609 2.5 7.5 0.3
O1 A:OXY609 2.7 6.2 0.3
O A:HOH701 2.8 7.7 0.3
CE1 A:HIS402 2.8 6.1 1.0
CD2 A:HIS452 2.9 8.0 1.0
CE1 A:HIS112 2.9 7.4 1.0
HE1 A:HIS402 3.0 6.1 1.0
CE1 A:HIS452 3.0 8.8 1.0
HD2 A:HIS452 3.0 8.0 1.0
HE1 A:HIS112 3.0 7.1 1.0
CD2 A:HIS402 3.1 5.8 1.0
CD2 A:HIS112 3.1 6.8 1.0
HD2 A:PHE450 3.2 7.7 1.0
HE1 A:HIS452 3.2 8.5 1.0
O A:HOH705 3.3 11.9 0.3
HD2 A:HIS112 3.4 6.8 1.0
HD2 A:HIS402 3.4 5.9 1.0
HD2 A:HIS400 3.4 6.2 1.0
HB3 A:PHE450 3.6 6.7 1.0
CD2 A:PHE450 3.9 7.8 1.0
O A:HOH702 3.9 10.0 0.5
ND1 A:HIS402 4.0 6.2 1.0
HB3 A:PRO80 4.0 6.2 1.0
CG A:HIS452 4.0 7.4 1.0
ND1 A:HIS452 4.0 7.7 1.0
ND1 A:HIS112 4.1 6.7 1.0
CG A:HIS402 4.2 5.9 1.0
CG A:HIS112 4.2 6.5 1.0
CD2 A:HIS400 4.3 6.3 1.0
O1 A:OXY610 4.3 15.3 0.5
CB A:PHE450 4.4 6.8 1.0
HE1 A:HIS110 4.4 6.2 1.0
CU A:CU603 4.4 6.4 0.8
HD21 A:LEU459 4.4 8.0 1.0
HB2 A:PHE450 4.5 6.7 1.0
HD2 A:HIS65 4.5 6.4 1.0
CG A:PHE450 4.5 6.9 1.0
CD2 A:HIS65 4.6 6.2 1.0
HE2 A:PHE450 4.6 8.0 1.0
NE2 A:HIS65 4.7 6.5 1.0
CE2 A:PHE450 4.7 8.2 1.0
HD1 A:HIS402 4.8 6.1 1.0
NE2 A:HIS400 4.8 6.1 1.0
HD1 A:HIS452 4.8 7.9 1.0
HD1 A:HIS112 4.9 6.8 1.0
CU A:CU602 4.9 12.3 0.4
HD22 A:LEU459 5.0 8.0 1.0
O2 A:OXY610 5.0 15.4 0.5
CB A:PRO80 5.0 6.1 1.0

Copper binding site 3 out of 6 in 5mi2

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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 10-Th Structure of the Series with Total Exposition Time 273 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 10-Th Structure of the Series with Total Exposition Time 273 Min. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu602

b:12.3
occ:0.40
 CU A:CU602 0.0 12.3 0.4
CU A:CU602 0.4 4.2 0.5
ND1 A:HIS67 2.0 6.0 1.0
NE2 A:HIS454 2.1 6.8 1.0
NE2 A:HIS110 2.1 6.5 1.0
O A:HOH701 2.2 7.7 0.3
O1 A:OXY609 2.3 6.2 0.3
O A:HOH705 2.4 11.9 0.3
O A:HOH704 2.6 4.7 0.3
O2 A:OXY609 2.8 7.5 0.3
HD2 A:HIS65 2.8 6.4 1.0
HB2 A:HIS67 2.9 5.7 1.0
CE1 A:HIS110 3.0 6.4 1.0
CE1 A:HIS67 3.0 5.8 1.0
HE1 A:HIS110 3.1 6.2 1.0
CE1 A:HIS454 3.1 6.6 1.0
CD2 A:HIS454 3.1 6.4 1.0
HE1 A:HIS67 3.1 5.9 1.0
CG A:HIS67 3.1 5.4 1.0
CD2 A:HIS110 3.2 6.0 1.0
HE1 A:HIS454 3.3 6.5 1.0
HD2 A:HIS454 3.3 6.4 1.0
HD2 A:HIS110 3.5 6.1 1.0
CB A:HIS67 3.5 5.8 1.0
CD2 A:HIS65 3.6 6.2 1.0
CU A:CU603 3.7 6.4 0.8
HZ2 A:TRP108 3.9 6.0 1.0
HB2 A:ALA244 3.9 5.5 1.0
HD2 A:HIS400 4.0 6.2 1.0
NE2 A:HIS65 4.1 6.5 1.0
NE2 A:HIS67 4.1 6.2 1.0
NE2 A:HIS400 4.1 6.1 1.0
CD2 A:HIS400 4.1 6.3 1.0
ND1 A:HIS110 4.2 5.6 1.0
CZ2 A:TRP108 4.2 6.1 1.0
HB3 A:HIS67 4.2 5.7 1.0
O A:HOH702 4.2 10.0 0.5
ND1 A:HIS454 4.2 6.0 1.0
CD2 A:HIS67 4.2 6.3 1.0
CG A:HIS454 4.2 6.0 1.0
HA A:HIS67 4.3 5.7 1.0
CU A:CU601 4.3 8.0 0.4
CG A:HIS110 4.3 5.8 1.0
HE1 A:TRP108 4.4 5.8 1.0
CE2 A:TRP108 4.4 5.8 1.0
NE1 A:TRP108 4.5 5.7 1.0
CA A:HIS67 4.6 5.7 1.0
HB1 A:ALA244 4.6 5.5 1.0
CB A:ALA244 4.6 5.6 1.0
HD2 A:HIS112 4.7 6.8 1.0
HE1 A:HIS452 4.7 8.5 1.0
O1 A:OXY610 4.8 15.3 0.5
CG A:HIS65 4.9 6.4 1.0
HE2 A:HIS67 4.9 6.1 1.0
HD1 A:HIS110 4.9 5.8 1.0
CH2 A:TRP108 4.9 6.0 1.0
CU A:CU601 4.9 5.5 0.5
CE1 A:HIS400 5.0 6.1 1.0
HD1 A:HIS454 5.0 6.2 1.0
CG A:HIS400 5.0 5.9 1.0
HB3 A:ALA244 5.0 5.5 1.0

Copper binding site 4 out of 6 in 5mi2

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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 10-Th Structure of the Series with Total Exposition Time 273 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 10-Th Structure of the Series with Total Exposition Time 273 Min. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu602

b:4.2
occ:0.50
 CU A:CU602 0.0 4.2 0.5
CU A:CU602 0.4 12.3 0.4
ND1 A:HIS67 1.9 6.0 1.0
NE2 A:HIS110 2.0 6.5 1.0
NE2 A:HIS454 2.1 6.8 1.0
O A:HOH701 2.6 7.7 0.3
O1 A:OXY609 2.7 6.2 0.3
HB2 A:HIS67 2.8 5.7 1.0
O A:HOH705 2.8 11.9 0.3
CE1 A:HIS67 2.9 5.8 1.0
CE1 A:HIS454 3.0 6.6 1.0
CD2 A:HIS110 3.0 6.0 1.0
CG A:HIS67 3.0 5.4 1.0
CE1 A:HIS110 3.0 6.4 1.0
O A:HOH704 3.0 4.7 0.3
HD2 A:HIS65 3.1 6.4 1.0
HE1 A:HIS454 3.1 6.5 1.0
HE1 A:HIS67 3.1 5.9 1.0
HD2 A:HIS110 3.2 6.1 1.0
CD2 A:HIS454 3.2 6.4 1.0
O2 A:OXY609 3.2 7.5 0.3
HE1 A:HIS110 3.2 6.2 1.0
CB A:HIS67 3.4 5.8 1.0
HD2 A:HIS454 3.4 6.4 1.0
HZ2 A:TRP108 3.5 6.0 1.0
HB2 A:ALA244 3.6 5.5 1.0
CZ2 A:TRP108 3.7 6.1 1.0
CD2 A:HIS65 3.9 6.2 1.0
HB3 A:HIS67 4.0 5.7 1.0
HE1 A:TRP108 4.0 5.8 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 6.4 0.8
CD2 A:HIS67 4.1 6.3 1.0
NE1 A:TRP108 4.1 5.7 1.0
ND1 A:HIS110 4.1 5.6 1.0
ND1 A:HIS454 4.1 6.0 1.0
CG A:HIS110 4.1 5.8 1.0
CG A:HIS454 4.3 6.0 1.0
HD2 A:HIS400 4.3 6.2 1.0
HA A:HIS67 4.3 5.7 1.0
HB1 A:ALA244 4.3 5.5 1.0
CB A:ALA244 4.4 5.6 1.0
NE2 A:HIS65 4.4 6.5 1.0
O A:HOH702 4.4 10.0 0.5
NE2 A:HIS400 4.4 6.1 1.0
CD2 A:HIS400 4.5 6.3 1.0
CA A:HIS67 4.5 5.7 1.0
CH2 A:TRP108 4.5 6.0 1.0
HH2 A:TRP108 4.7 6.1 1.0
CU A:CU601 4.7 8.0 0.4
HB3 A:ALA244 4.8 5.5 1.0
HE2 A:HIS67 4.8 6.1 1.0
CD2 A:TRP108 4.9 5.6 1.0
HD1 A:HIS454 4.9 6.2 1.0
HD1 A:HIS110 4.9 5.8 1.0
HD2 A:HIS67 5.0 6.1 1.0
HD2 A:HIS112 5.0 6.8 1.0

Copper binding site 5 out of 6 in 5mi2

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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 10-Th Structure of the Series with Total Exposition Time 273 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 10-Th Structure of the Series with Total Exposition Time 273 Min. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu603

b:6.4
occ:0.80
 O A:HOH705 1.9 11.9 0.3
NE2 A:HIS400 1.9 6.1 1.0
NE2 A:HIS65 1.9 6.5 1.0
O A:HOH1082 2.1 5.4 0.3
O A:HOH1103 2.8 5.4 0.7
CE1 A:HIS65 2.9 6.5 1.0
CD2 A:HIS400 2.9 6.3 1.0
CE1 A:HIS400 2.9 6.1 1.0
CD2 A:HIS65 2.9 6.2 1.0
O1 A:OXY609 3.0 6.2 0.3
HE1 A:HIS65 3.1 6.5 1.0
HA A:HIS67 3.1 5.7 1.0
HD2 A:HIS400 3.1 6.2 1.0
HE1 A:HIS400 3.1 6.1 1.0
HD2 A:HIS65 3.1 6.4 1.0
O A:HOH704 3.2 4.7 0.3
H A:GLY68 3.3 5.7 1.0
CD2 A:HIS402 3.4 5.8 1.0
NE2 A:HIS402 3.5 6.3 1.0
ND1 A:HIS67 3.5 6.0 1.0
O A:HOH701 3.5 7.7 0.3
HD2 A:HIS402 3.6 5.9 1.0
HA A:HIS402 3.7 5.8 1.0
CU A:CU602 3.7 12.3 0.4
CG A:HIS402 3.8 5.9 1.0
CE1 A:HIS402 3.8 6.1 1.0
CG A:HIS67 3.8 5.4 1.0
CE1 A:HIS67 3.9 5.8 1.0
CU A:CU601 3.9 8.0 0.4
CA A:HIS67 4.0 5.7 1.0
ND1 A:HIS65 4.0 6.6 1.0
ND1 A:HIS402 4.0 6.2 1.0
ND1 A:HIS400 4.0 5.9 1.0
CG A:HIS400 4.0 5.9 1.0
CG A:HIS65 4.0 6.4 1.0
CU A:CU602 4.1 4.2 0.5
N A:GLY68 4.1 5.4 1.0
HB2 A:HIS67 4.1 5.7 1.0
HE1 A:HIS67 4.2 5.9 1.0
CB A:HIS67 4.2 5.8 1.0
O2 A:OXY609 4.2 7.5 0.3
HE1 A:HIS402 4.3 6.1 1.0
NE2 A:HIS67 4.4 6.2 1.0
CD2 A:HIS67 4.4 6.3 1.0
CU A:CU601 4.4 5.5 0.5
CA A:HIS402 4.5 5.8 1.0
HD1 A:HIS402 4.5 6.1 1.0
C A:HIS67 4.6 5.8 1.0
CB A:HIS402 4.6 6.0 1.0
O A:HOH937 4.7 10.1 1.0
HD1 A:HIS65 4.7 6.5 1.0
HD1 A:HIS400 4.8 5.9 1.0
HB3 A:HIS402 4.8 5.9 1.0
O A:HOH822 4.8 9.2 1.0
N A:HIS402 4.9 5.7 1.0
HD2 A:HIS454 4.9 6.4 1.0
HD2 A:HIS112 4.9 6.8 1.0
HA2 A:GLY68 4.9 5.9 1.0
HE2 A:HIS67 5.0 6.1 1.0
HD2 A:HIS67 5.0 6.1 1.0
O A:LEU401 5.0 6.4 1.0

Copper binding site 6 out of 6 in 5mi2

Go back to Copper Binding Sites List in 5mi2
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 10-Th Structure of the Series with Total Exposition Time 273 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 10-Th Structure of the Series with Total Exposition Time 273 Min. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu604

b:5.9
occ:0.90
 ND1 A:HIS458 2.0 6.6 1.0
ND1 A:HIS397 2.0 6.5 1.0
SG A:CYS453 2.2 6.7 1.0
HD11 A:ILE455 2.7 6.0 1.0
CE1 A:HIS397 3.0 6.8 1.0
CE1 A:HIS458 3.0 7.2 1.0
HB A:ILE455 3.0 6.2 1.0
HD2 A:PHE463 3.0 6.7 1.0
CG A:HIS458 3.1 6.8 1.0
HB3 A:HIS397 3.1 6.5 1.0
CG A:HIS397 3.1 6.3 1.0
HE1 A:HIS397 3.1 6.8 1.0
HB2 A:HIS458 3.1 7.1 1.0
HE1 A:HIS458 3.2 7.2 1.0
CB A:CYS453 3.3 6.9 1.0
HB3 A:HIS458 3.3 7.1 1.0
HB2 A:CYS453 3.3 6.7 1.0
CB A:HIS458 3.4 7.1 1.0
HA A:HIS397 3.4 6.5 1.0
HB3 A:CYS453 3.4 6.7 1.0
CB A:HIS397 3.5 6.6 1.0
HE2 A:PHE463 3.5 6.8 1.0
CD1 A:ILE455 3.6 6.0 1.0
HD2 A:PRO398 3.8 6.2 1.0
CD2 A:PHE463 3.8 6.6 1.0
CB A:ILE455 3.9 6.0 1.0
H A:ILE455 3.9 6.7 1.0
HD12 A:ILE455 3.9 6.0 1.0
CA A:HIS397 4.0 6.6 1.0
CG1 A:ILE455 4.0 6.2 1.0
CE2 A:PHE463 4.1 6.8 1.0
HG13 A:ILE455 4.1 6.1 1.0
NE2 A:HIS397 4.1 7.2 1.0
NE2 A:HIS458 4.1 7.7 1.0
CD2 A:HIS458 4.2 6.7 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 6.5 1.0
HG21 A:ILE455 4.6 6.3 1.0
HG22 A:ILE455 4.6 6.3 1.0
O A:GLY394 4.6 9.4 1.0
HZ A:PHE341 4.6 8.1 1.0
CD A:PRO398 4.6 6.2 1.0
CG2 A:ILE455 4.6 6.4 1.0
CA A:CYS453 4.7 6.4 1.0
CZ A:PHE341 4.8 8.2 1.0
N A:ILE455 4.8 6.7 1.0
HA A:CYS453 4.8 6.4 1.0
HD3 A:PRO398 4.8 6.2 1.0
HE1 A:PHE399 4.8 7.5 1.0
HE2 A:HIS397 4.9 7.1 1.0
HE2 A:PHE341 4.9 8.0 1.0
CE2 A:PHE341 4.9 8.0 1.0
HE2 A:HIS458 4.9 7.3 1.0
CA A:HIS458 4.9 7.4 1.0
CA A:ILE455 4.9 6.4 1.0
C A:HIS397 5.0 6.3 1.0
O A:ILE455 5.0 6.5 1.0
N A:HIS397 5.0 6.5 1.0
HG12 A:ILE455 5.0 6.1 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

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