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Copper in PDB 5mej: Structural Study of the X-Ray Induced Enzymatic Reduction of Molecular Oxygen to Water For Laccase From Steccherinum Murashkinskyi. First Structure of the Series with 3 Min Total X-Ray Exposition Time.

Enzymatic activity of Structural Study of the X-Ray Induced Enzymatic Reduction of Molecular Oxygen to Water For Laccase From Steccherinum Murashkinskyi. First Structure of the Series with 3 Min Total X-Ray Exposition Time.

All present enzymatic activity of Structural Study of the X-Ray Induced Enzymatic Reduction of Molecular Oxygen to Water For Laccase From Steccherinum Murashkinskyi. First Structure of the Series with 3 Min Total X-Ray Exposition Time.:
1.10.3.2;

Protein crystallography data

The structure of Structural Study of the X-Ray Induced Enzymatic Reduction of Molecular Oxygen to Water For Laccase From Steccherinum Murashkinskyi. First Structure of the Series with 3 Min Total X-Ray Exposition Time., PDB code: 5mej was solved by K.M.Polyakov, T.V.Fedorova, S.Gavryushov, A.N.Popov, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 67.57 / 1.50
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 (%) 13.9 / 16.1

Other elements in 5mej:

The structure of Structural Study of the X-Ray Induced Enzymatic Reduction of Molecular Oxygen to Water For Laccase From Steccherinum Murashkinskyi. First Structure of the Series with 3 Min Total X-Ray Exposition Time. also contains other interesting chemical elements:

Sodium (Na) 1 atom

Copper Binding Sites:

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

Copper binding site 1 out of 6 in 5mej

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Copper binding site 1 out of 6 in the Structural Study of the X-Ray Induced Enzymatic Reduction of Molecular Oxygen to Water For Laccase From Steccherinum Murashkinskyi. First Structure of the Series with 3 Min Total X-Ray Exposition Time.


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Structural Study of the X-Ray Induced Enzymatic Reduction of Molecular Oxygen to Water For Laccase From Steccherinum Murashkinskyi. First Structure of the Series with 3 Min Total X-Ray Exposition Time. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu501

b:6.5
occ:0.60
 CU A:CU501 0.0 6.5 0.6
CU A:CU501 0.8 7.8 0.3
O1 A:OXY511 1.4 4.5 0.3
O A:HOH601 1.8 5.0 0.6
NE2 A:HIS402 2.0 7.0 1.0
NE2 A:HIS452 2.1 9.3 1.0
NE2 A:HIS112 2.1 6.9 1.0
O2 A:OXY511 2.1 4.7 0.3
O A:HOH608 2.4 9.0 0.6
CE1 A:HIS402 2.9 7.1 1.0
CE1 A:HIS452 3.0 9.5 1.0
HD2 A:HIS400 3.0 6.9 1.0
HE1 A:HIS402 3.0 7.0 1.0
CD2 A:HIS112 3.0 7.2 1.0
HE1 A:HIS452 3.1 9.2 1.0
HD2 A:HIS112 3.1 7.3 1.0
CD2 A:HIS402 3.1 6.5 1.0
CE1 A:HIS112 3.2 7.7 1.0
CD2 A:HIS452 3.2 8.4 1.0
HD2 A:HIS402 3.4 6.6 1.0
HE1 A:HIS112 3.4 7.4 1.0
HD2 A:HIS452 3.4 8.6 1.0
CU A:CU502 3.7 10.4 0.6
HD2 A:HIS65 3.7 7.5 1.0
HE1 A:HIS110 3.7 7.7 1.0
CD2 A:HIS400 3.8 7.0 1.0
CU A:CU503 3.9 6.6 0.8
O A:HOH602 3.9 10.9 0.5
CD2 A:HIS65 3.9 7.5 1.0
ND1 A:HIS402 4.0 6.7 1.0
HD2 A:PHE450 4.0 8.3 1.0
NE2 A:HIS65 4.1 7.8 1.0
O1 A:OXY512 4.1 13.6 0.5
ND1 A:HIS452 4.2 8.8 1.0
CG A:HIS402 4.2 6.2 1.0
CG A:HIS112 4.2 7.8 1.0
ND1 A:HIS112 4.3 7.4 1.0
CG A:HIS452 4.3 8.3 1.0
NE2 A:HIS400 4.3 6.7 1.0
HB3 A:PHE450 4.3 7.5 1.0
CE1 A:HIS110 4.5 8.0 1.0
HB3 A:PRO80 4.5 7.0 1.0
HD2 A:HIS454 4.6 7.2 1.0
NE2 A:HIS454 4.6 7.2 1.0
CU A:CU502 4.6 5.6 0.3
O2 A:OXY512 4.7 13.4 0.5
CG A:HIS65 4.7 7.3 1.0
CD2 A:HIS454 4.8 7.3 1.0
NE2 A:HIS110 4.8 7.5 1.0
CD2 A:PHE450 4.8 8.6 1.0
HD1 A:HIS402 4.8 6.6 1.0
CE1 A:HIS65 4.9 7.9 1.0
HD21 A:LEU459 4.9 8.7 1.0
HD1 A:HIS452 4.9 8.8 1.0

Copper binding site 2 out of 6 in 5mej

Go back to Copper Binding Sites List in 5mej
Copper binding site 2 out of 6 in the Structural Study of the X-Ray Induced Enzymatic Reduction of Molecular Oxygen to Water For Laccase From Steccherinum Murashkinskyi. First Structure of the Series with 3 Min Total X-Ray Exposition Time.


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of Structural Study of the X-Ray Induced Enzymatic Reduction of Molecular Oxygen to Water For Laccase From Steccherinum Murashkinskyi. First Structure of the Series with 3 Min Total X-Ray Exposition Time. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu501

b:7.8
occ:0.30
 CU A:CU501 0.0 7.8 0.3
CU A:CU501 0.8 6.5 0.6
NE2 A:HIS452 1.9 9.3 1.0
NE2 A:HIS402 1.9 7.0 1.0
NE2 A:HIS112 1.9 6.9 1.0
O1 A:OXY511 2.1 4.5 0.3
O A:HOH601 2.4 5.0 0.6
O2 A:OXY511 2.7 4.7 0.3
CD2 A:HIS452 2.7 8.4 1.0
CE1 A:HIS402 2.8 7.1 1.0
CE1 A:HIS112 2.8 7.7 1.0
HD2 A:HIS452 2.9 8.6 1.0
HE1 A:HIS112 2.9 7.4 1.0
HE1 A:HIS402 2.9 7.0 1.0
CE1 A:HIS452 2.9 9.5 1.0
CD2 A:HIS402 3.0 6.5 1.0
CD2 A:HIS112 3.1 7.2 1.0
O A:HOH608 3.1 9.0 0.6
HE1 A:HIS452 3.3 9.2 1.0
HD2 A:PHE450 3.3 8.3 1.0
HD2 A:HIS402 3.3 6.6 1.0
HD2 A:HIS112 3.4 7.3 1.0
HD2 A:HIS400 3.4 6.9 1.0
HB3 A:PHE450 3.7 7.5 1.0
CG A:HIS452 3.9 8.3 1.0
ND1 A:HIS402 3.9 6.7 1.0
ND1 A:HIS452 3.9 8.8 1.0
ND1 A:HIS112 4.0 7.4 1.0
CD2 A:PHE450 4.0 8.6 1.0
CG A:HIS402 4.1 6.2 1.0
HB3 A:PRO80 4.1 7.0 1.0
CG A:HIS112 4.1 7.8 1.0
O A:HOH602 4.1 10.9 0.5
HE1 A:HIS110 4.2 7.7 1.0
CD2 A:HIS400 4.3 7.0 1.0
O1 A:OXY512 4.3 13.6 0.5
HD2 A:HIS65 4.4 7.5 1.0
CU A:CU503 4.4 6.6 0.8
CU A:CU502 4.5 10.4 0.6
CD2 A:HIS65 4.5 7.5 1.0
HD21 A:LEU459 4.5 8.7 1.0
CB A:PHE450 4.5 7.8 1.0
NE2 A:HIS65 4.6 7.8 1.0
CG A:PHE450 4.7 7.6 1.0
HD1 A:HIS402 4.7 6.6 1.0
HE2 A:PHE450 4.7 8.6 1.0
HD1 A:HIS112 4.7 7.5 1.0
HB2 A:PHE450 4.7 7.5 1.0
HD1 A:HIS452 4.7 8.8 1.0
CE2 A:PHE450 4.8 8.4 1.0
O2 A:OXY512 4.8 13.4 0.5
NE2 A:HIS400 4.8 6.7 1.0

Copper binding site 3 out of 6 in 5mej

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Copper binding site 3 out of 6 in the Structural Study of the X-Ray Induced Enzymatic Reduction of Molecular Oxygen to Water For Laccase From Steccherinum Murashkinskyi. First Structure of the Series with 3 Min Total X-Ray Exposition Time.


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 3 of Structural Study of the X-Ray Induced Enzymatic Reduction of Molecular Oxygen to Water For Laccase From Steccherinum Murashkinskyi. First Structure of the Series with 3 Min Total X-Ray Exposition Time. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu502

b:10.4
occ:0.60
 CU A:CU502 0.0 10.4 0.6
CU A:CU502 0.9 5.6 0.3
NE2 A:HIS454 2.1 7.2 1.0
ND1 A:HIS67 2.1 7.4 1.0
O A:HOH601 2.2 5.0 0.6
NE2 A:HIS110 2.2 7.5 1.0
O A:HOH608 2.2 9.0 0.6
O1 A:OXY511 2.3 4.5 0.3
O2 A:OXY511 2.5 4.7 0.3
HD2 A:HIS65 2.8 7.5 1.0
CE1 A:HIS67 3.0 6.8 1.0
CE1 A:HIS110 3.0 8.0 1.0
CD2 A:HIS454 3.0 7.3 1.0
HE1 A:HIS67 3.0 7.0 1.0
HE1 A:HIS110 3.1 7.7 1.0
CE1 A:HIS454 3.1 7.2 1.0
HB2 A:HIS67 3.1 6.6 1.0
HD2 A:HIS454 3.2 7.2 1.0
CG A:HIS67 3.2 6.7 1.0
HE1 A:HIS454 3.3 7.1 1.0
CD2 A:HIS110 3.3 7.0 1.0
HD2 A:HIS110 3.6 7.1 1.0
CD2 A:HIS65 3.6 7.5 1.0
HD2 A:HIS400 3.6 6.9 1.0
CU A:CU503 3.7 6.6 0.8
CB A:HIS67 3.7 6.5 1.0
CU A:CU501 3.7 6.5 0.6
CD2 A:HIS400 3.9 7.0 1.0
NE2 A:HIS400 4.0 6.7 1.0
NE2 A:HIS65 4.1 7.8 1.0
HB2 A:ALA244 4.1 5.8 1.0
HZ2 A:TRP108 4.1 6.6 1.0
NE2 A:HIS67 4.1 7.0 1.0
HE1 A:HIS452 4.2 9.2 1.0
ND1 A:HIS454 4.2 6.8 1.0
O A:HOH602 4.2 10.9 0.5
ND1 A:HIS110 4.2 7.6 1.0
CG A:HIS454 4.2 7.0 1.0
CD2 A:HIS67 4.3 7.0 1.0
HB3 A:HIS67 4.4 6.6 1.0
CG A:HIS110 4.4 7.1 1.0
HA A:HIS67 4.4 6.6 1.0
HD2 A:HIS112 4.4 7.3 1.0
CZ2 A:TRP108 4.5 6.7 1.0
CU A:CU501 4.5 7.8 0.3
O1 A:OXY512 4.6 13.6 0.5
HE1 A:TRP108 4.7 6.6 1.0
CA A:HIS67 4.7 6.7 1.0
HB1 A:ALA244 4.7 5.8 1.0
CE2 A:TRP108 4.8 6.5 1.0
CE1 A:HIS452 4.8 9.5 1.0
CG A:HIS400 4.8 6.9 1.0
CB A:ALA244 4.8 5.8 1.0
NE2 A:HIS452 4.9 9.3 1.0
CG A:HIS65 4.9 7.3 1.0
NE1 A:TRP108 4.9 6.6 1.0
HE2 A:HIS67 4.9 6.9 1.0
HD1 A:HIS110 4.9 7.6 1.0
CD2 A:HIS112 4.9 7.2 1.0
HD1 A:HIS454 5.0 7.0 1.0
CE1 A:HIS400 5.0 7.0 1.0
NE2 A:HIS112 5.0 6.9 1.0

Copper binding site 4 out of 6 in 5mej

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Copper binding site 4 out of 6 in the Structural Study of the X-Ray Induced Enzymatic Reduction of Molecular Oxygen to Water For Laccase From Steccherinum Murashkinskyi. First Structure of the Series with 3 Min Total X-Ray Exposition Time.


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 4 of Structural Study of the X-Ray Induced Enzymatic Reduction of Molecular Oxygen to Water For Laccase From Steccherinum Murashkinskyi. First Structure of the Series with 3 Min Total X-Ray Exposition Time. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu502

b:5.6
occ:0.30
 CU A:CU502 0.0 5.6 0.3
CU A:CU502 0.9 10.4 0.6
ND1 A:HIS67 1.9 7.4 1.0
NE2 A:HIS110 1.9 7.5 1.0
NE2 A:HIS454 2.1 7.2 1.0
CD2 A:HIS110 2.8 7.0 1.0
HB2 A:HIS67 2.8 6.6 1.0
CE1 A:HIS67 2.9 6.8 1.0
CE1 A:HIS454 2.9 7.2 1.0
HD2 A:HIS110 2.9 7.1 1.0
CG A:HIS67 2.9 6.7 1.0
HE1 A:HIS454 3.0 7.1 1.0
O A:HOH601 3.0 5.0 0.6
O A:HOH608 3.0 9.0 0.6
CE1 A:HIS110 3.1 8.0 1.0
HE1 A:HIS67 3.1 7.0 1.0
O2 A:OXY511 3.2 4.7 0.3
O1 A:OXY511 3.2 4.5 0.3
CD2 A:HIS454 3.2 7.3 1.0
HD2 A:HIS65 3.3 7.5 1.0
CB A:HIS67 3.3 6.5 1.0
HZ2 A:TRP108 3.3 6.6 1.0
HE1 A:HIS110 3.4 7.7 1.0
HB2 A:ALA244 3.5 5.8 1.0
HD2 A:HIS454 3.5 7.2 1.0
CZ2 A:TRP108 3.6 6.7 1.0
HB3 A:HIS67 3.8 6.6 1.0
CE2 A:TRP108 3.9 6.5 1.0
HE1 A:TRP108 3.9 6.6 1.0
NE2 A:HIS67 3.9 7.0 1.0
CG A:HIS110 4.0 7.1 1.0
CD2 A:HIS67 4.0 7.0 1.0
NE1 A:TRP108 4.0 6.6 1.0
ND1 A:HIS110 4.1 7.6 1.0
ND1 A:HIS454 4.1 6.8 1.0
CD2 A:HIS65 4.1 7.5 1.0
CG A:HIS454 4.3 7.0 1.0
HB1 A:ALA244 4.3 5.8 1.0
CU A:CU503 4.3 6.6 0.8
CB A:ALA244 4.3 5.8 1.0
CH2 A:TRP108 4.3 6.6 1.0
HD2 A:HIS400 4.4 6.9 1.0
HA A:HIS67 4.4 6.6 1.0
HH2 A:TRP108 4.5 6.7 1.0
CA A:HIS67 4.6 6.7 1.0
CD2 A:HIS400 4.6 7.0 1.0
NE2 A:HIS65 4.6 7.8 1.0
O A:HOH602 4.6 10.9 0.5
NE2 A:HIS400 4.6 6.7 1.0
CU A:CU501 4.6 6.5 0.6
HE2 A:HIS67 4.7 6.9 1.0
CD2 A:TRP108 4.7 6.5 1.0
HB3 A:ALA244 4.8 5.8 1.0
HD1 A:HIS454 4.8 7.0 1.0
HE1 A:HIS452 4.8 9.2 1.0
HD2 A:HIS67 4.9 6.9 1.0
HD1 A:HIS110 4.9 7.6 1.0
CD1 A:TRP108 5.0 6.6 1.0

Copper binding site 5 out of 6 in 5mej

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Copper binding site 5 out of 6 in the Structural Study of the X-Ray Induced Enzymatic Reduction of Molecular Oxygen to Water For Laccase From Steccherinum Murashkinskyi. First Structure of the Series with 3 Min Total X-Ray Exposition Time.


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 5 of Structural Study of the X-Ray Induced Enzymatic Reduction of Molecular Oxygen to Water For Laccase From Steccherinum Murashkinskyi. First Structure of the Series with 3 Min Total X-Ray Exposition Time. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu503

b:6.6
occ:0.80
 NE2 A:HIS400 1.9 6.7 1.0
NE2 A:HIS65 1.9 7.8 1.0
O A:HOH608 1.9 9.0 0.6
O A:HOH1041 2.2 7.4 1.0
CE1 A:HIS65 2.9 7.9 1.0
CD2 A:HIS400 2.9 7.0 1.0
CE1 A:HIS400 2.9 7.0 1.0
CD2 A:HIS65 2.9 7.5 1.0
HA A:HIS67 3.0 6.6 1.0
HE1 A:HIS65 3.0 7.8 1.0
HD2 A:HIS400 3.1 6.9 1.0
HE1 A:HIS400 3.1 6.9 1.0
HD2 A:HIS65 3.2 7.5 1.0
H A:GLY68 3.3 6.4 1.0
CD2 A:HIS402 3.4 6.5 1.0
NE2 A:HIS402 3.5 7.0 1.0
ND1 A:HIS67 3.5 7.4 1.0
O1 A:OXY511 3.5 4.5 0.3
HD2 A:HIS402 3.6 6.6 1.0
HA A:HIS402 3.6 6.3 1.0
CU A:CU502 3.7 10.4 0.6
CG A:HIS402 3.7 6.2 1.0
CG A:HIS67 3.8 6.7 1.0
CU A:CU501 3.9 6.5 0.6
CE1 A:HIS402 3.9 7.1 1.0
CA A:HIS67 3.9 6.7 1.0
O A:HOH601 3.9 5.0 0.6
CE1 A:HIS67 3.9 6.8 1.0
ND1 A:HIS65 4.0 7.8 1.0
ND1 A:HIS400 4.0 6.8 1.0
ND1 A:HIS402 4.0 6.7 1.0
CG A:HIS400 4.0 6.9 1.0
N A:GLY68 4.0 6.2 1.0
CG A:HIS65 4.1 7.3 1.0
HB2 A:HIS67 4.1 6.6 1.0
CB A:HIS67 4.2 6.5 1.0
HE1 A:HIS67 4.2 7.0 1.0
CU A:CU502 4.3 5.6 0.3
CD2 A:HIS67 4.3 7.0 1.0
CA A:HIS402 4.4 6.2 1.0
NE2 A:HIS67 4.4 7.0 1.0
HE1 A:HIS402 4.4 7.0 1.0
CU A:CU501 4.4 7.8 0.3
C A:HIS67 4.5 6.7 1.0
CB A:HIS402 4.5 6.1 1.0
HD1 A:HIS402 4.6 6.6 1.0
O A:HOH921 4.6 11.6 1.0
O2 A:OXY511 4.6 4.7 0.3
O A:HOH784 4.7 9.4 1.0
HB3 A:HIS402 4.8 6.1 1.0
HD1 A:HIS65 4.8 7.7 1.0
HD1 A:HIS400 4.8 6.9 1.0
HA2 A:GLY68 4.8 6.7 1.0
N A:HIS402 4.8 6.4 1.0
HD2 A:HIS67 4.9 6.9 1.0
HE2 A:HIS67 4.9 6.9 1.0
HD2 A:HIS112 5.0 7.3 1.0
O A:LEU401 5.0 6.5 1.0
N A:HIS67 5.0 6.3 1.0
O A:TRP66 5.0 6.7 1.0

Copper binding site 6 out of 6 in 5mej

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


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 6 of Structural Study of the X-Ray Induced Enzymatic Reduction of Molecular Oxygen to Water For Laccase From Steccherinum Murashkinskyi. First Structure of the Series with 3 Min Total X-Ray Exposition Time. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu504

b:6.9
occ:0.90
 ND1 A:HIS458 2.0 8.0 1.0
ND1 A:HIS397 2.0 6.9 1.0
SG A:CYS453 2.1 7.7 1.0
HD11 A:ILE455 2.7 7.0 1.0
CE1 A:HIS397 2.9 7.2 1.0
CE1 A:HIS458 3.0 8.7 1.0
HD2 A:PHE463 3.0 7.0 1.0
CG A:HIS458 3.0 8.9 1.0
HB3 A:HIS397 3.0 7.8 1.0
CG A:HIS397 3.0 7.3 1.0
HE1 A:HIS397 3.1 7.3 1.0
HB2 A:HIS458 3.1 8.6 1.0
HB A:ILE455 3.1 7.0 1.0
HE1 A:HIS458 3.1 8.6 1.0
CB A:CYS453 3.3 7.5 1.0
HB3 A:HIS458 3.3 8.6 1.0
HB2 A:CYS453 3.3 7.5 1.0
CB A:HIS458 3.4 8.5 1.0
HB3 A:CYS453 3.4 7.5 1.0
HA A:HIS397 3.5 7.8 1.0
CB A:HIS397 3.5 7.9 1.0
HE2 A:PHE463 3.5 7.2 1.0
CD1 A:ILE455 3.6 7.1 1.0
CD2 A:PHE463 3.8 6.8 1.0
HD2 A:PRO398 3.9 7.2 1.0
H A:ILE455 4.0 7.5 1.0
CE2 A:PHE463 4.0 7.4 1.0
CB A:ILE455 4.0 6.9 1.0
CA A:HIS397 4.0 7.9 1.0
NE2 A:HIS397 4.0 7.7 1.0
HD12 A:ILE455 4.1 7.0 1.0
NE2 A:HIS458 4.1 8.8 1.0
CD2 A:HIS458 4.1 8.2 1.0
CD2 A:HIS397 4.1 7.7 1.0
HD13 A:ILE455 4.1 7.0 1.0
CG1 A:ILE455 4.2 6.9 1.0
HB2 A:HIS397 4.3 7.8 1.0
HG13 A:ILE455 4.4 6.9 1.0
HZ A:PHE341 4.6 8.5 1.0
O A:GLY394 4.6 9.8 1.0
CA A:CYS453 4.6 7.2 1.0
HG21 A:ILE455 4.7 7.0 1.0
CD A:PRO398 4.7 7.2 1.0
HG22 A:ILE455 4.7 7.0 1.0
CZ A:PHE341 4.7 8.7 1.0
CG2 A:ILE455 4.8 7.0 1.0
HE1 A:PHE399 4.8 7.8 1.0
HA A:CYS453 4.8 7.3 1.0
HE2 A:HIS397 4.8 7.6 1.0
N A:ILE455 4.8 7.5 1.0
HD3 A:PRO398 4.8 7.2 1.0
HE2 A:HIS458 4.9 8.6 1.0
HE2 A:PHE341 4.9 8.6 1.0
CA A:HIS458 4.9 8.6 1.0
CE2 A:PHE341 4.9 8.4 1.0
HB3 A:PHE463 4.9 7.1 1.0
O A:ILE455 5.0 7.4 1.0
HD2 A:HIS458 5.0 8.6 1.0
CG A:PHE463 5.0 7.2 1.0
C A:HIS397 5.0 7.8 1.0
CA A:ILE455 5.0 7.4 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 04:29:24 2024

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