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

Copper in PDB 5mew: The Study of the X-Ray Induced Enzymatic Reduction of Molecular Oxygen to Water For Laccase From Steccherinum Murashkinskyi. Second Structure of the Series with Total Exposition Time 33 Min.

Enzymatic activity of The Study of the X-Ray Induced Enzymatic Reduction of Molecular Oxygen to Water For Laccase From Steccherinum Murashkinskyi. Second Structure of the Series with Total Exposition Time 33 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. Second Structure of the Series with Total Exposition Time 33 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. Second Structure of the Series with Total Exposition Time 33 Min., PDB code: 5mew was solved by K.M.Polyakov, T.N.Fedorova, S.Gavryushov, A.N.Popov, O.A.Glazunova, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.00 / 1.35
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 56.380, 84.400, 112.490, 90.00, 90.00, 90.00
R / Rfree (%) 13.2 / 15.2

Other elements in 5mew:

The structure of The Study of the X-Ray Induced Enzymatic Reduction of Molecular Oxygen to Water For Laccase From Steccherinum Murashkinskyi. Second Structure of the Series with Total Exposition Time 33 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. Second Structure of the Series with Total Exposition Time 33 Min. (pdb code 5mew). 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. Second Structure of the Series with Total Exposition Time 33 Min., PDB code: 5mew:
Jump to Copper binding site number: 1; 2; 3; 4; 5; 6;

Copper binding site 1 out of 6 in 5mew

Go back to Copper Binding Sites List in 5mew
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. Second Structure of the Series with Total Exposition Time 33 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. Second Structure of the Series with Total Exposition Time 33 Min. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu501

b:5.2
occ:0.50
 CU A:CU501 0.0 5.2 0.5
CU A:CU501 0.8 6.2 0.4
O1 A:OXY511 1.5 7.1 0.4
O A:HOH605 1.8 4.0 0.5
O2 A:OXY511 1.9 7.7 0.4
NE2 A:HIS402 2.1 6.5 1.0
NE2 A:HIS112 2.2 6.8 1.0
NE2 A:HIS452 2.2 9.1 1.0
O A:HOH605 2.4 6.5 0.5
CE1 A:HIS402 3.0 6.6 1.0
HD2 A:HIS400 3.0 6.5 1.0
CE1 A:HIS452 3.0 9.6 1.0
CD2 A:HIS112 3.0 6.8 1.0
HE1 A:HIS452 3.1 9.2 1.0
HE1 A:HIS402 3.1 6.5 1.0
HD2 A:HIS112 3.1 6.7 1.0
CD2 A:HIS402 3.1 6.1 1.0
CE1 A:HIS112 3.3 7.3 1.0
CD2 A:HIS452 3.3 8.4 1.0
HD2 A:HIS402 3.4 6.1 1.0
HE1 A:HIS112 3.5 7.0 1.0
HD2 A:HIS452 3.6 8.4 1.0
CU A:CU502 3.6 8.1 0.5
HE1 A:HIS110 3.7 7.3 1.0
O A:HOH607 3.7 23.0 0.5
HD2 A:HIS65 3.7 6.5 1.0
CU A:CU503 3.8 6.0 0.8
CD2 A:HIS400 3.8 6.6 1.0
CD2 A:HIS65 3.9 6.4 1.0
O1 A:OXY512 4.0 7.6 0.5
NE2 A:HIS65 4.0 6.5 1.0
HD2 A:PHE450 4.1 7.7 1.0
ND1 A:HIS402 4.1 6.2 1.0
CG A:HIS402 4.2 5.7 1.0
ND1 A:HIS452 4.2 8.3 1.0
CG A:HIS112 4.2 6.5 1.0
NE2 A:HIS400 4.3 6.5 1.0
ND1 A:HIS112 4.3 6.6 1.0
HB3 A:PHE450 4.4 6.5 1.0
CG A:HIS452 4.4 7.8 1.0
CE1 A:HIS110 4.5 7.5 1.0
CU A:CU502 4.5 5.4 0.4
HB3 A:PRO80 4.6 6.3 1.0
O2 A:OXY512 4.6 9.6 0.5
NE2 A:HIS454 4.6 6.9 1.0
HD2 A:HIS454 4.6 6.5 1.0
CG A:HIS65 4.7 6.6 1.0
CD2 A:HIS454 4.7 6.5 1.0
NE2 A:HIS110 4.8 7.4 1.0
CD2 A:PHE450 4.8 7.8 1.0
HD1 A:HIS402 4.8 6.2 1.0
CE1 A:HIS65 4.8 6.5 1.0
HD21 A:LEU459 4.9 8.5 1.0
HD1 A:HIS452 4.9 8.4 1.0

Copper binding site 2 out of 6 in 5mew

Go back to Copper Binding Sites List in 5mew
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. Second Structure of the Series with Total Exposition Time 33 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. Second Structure of the Series with Total Exposition Time 33 Min. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu501

b:6.2
occ:0.40
 CU A:CU501 0.0 6.2 0.4
CU A:CU501 0.8 5.2 0.5
NE2 A:HIS452 1.9 9.1 1.0
NE2 A:HIS112 1.9 6.8 1.0
NE2 A:HIS402 2.0 6.5 1.0
O1 A:OXY511 2.2 7.1 0.4
O2 A:OXY511 2.5 7.7 0.4
O A:HOH605 2.5 4.0 0.5
CD2 A:HIS452 2.8 8.4 1.0
CE1 A:HIS112 2.8 7.3 1.0
CE1 A:HIS402 2.8 6.6 1.0
CE1 A:HIS452 2.9 9.6 1.0
HE1 A:HIS112 2.9 7.0 1.0
HE1 A:HIS402 3.0 6.5 1.0
HD2 A:HIS452 3.0 8.4 1.0
CD2 A:HIS402 3.1 6.1 1.0
CD2 A:HIS112 3.1 6.8 1.0
O A:HOH605 3.1 6.5 0.5
HE1 A:HIS452 3.2 9.2 1.0
HD2 A:PHE450 3.3 7.7 1.0
HD2 A:HIS402 3.3 6.1 1.0
HD2 A:HIS112 3.4 6.7 1.0
HD2 A:HIS400 3.4 6.5 1.0
HB3 A:PHE450 3.8 6.5 1.0
O A:HOH607 3.9 23.0 0.5
ND1 A:HIS452 3.9 8.3 1.0
CG A:HIS452 3.9 7.8 1.0
ND1 A:HIS112 4.0 6.6 1.0
CD2 A:PHE450 4.0 7.8 1.0
ND1 A:HIS402 4.0 6.2 1.0
HB3 A:PRO80 4.1 6.3 1.0
CG A:HIS402 4.1 5.7 1.0
CG A:HIS112 4.2 6.5 1.0
HE1 A:HIS110 4.2 7.3 1.0
O1 A:OXY512 4.2 7.6 0.5
CD2 A:HIS400 4.3 6.6 1.0
CU A:CU502 4.4 8.1 0.5
CU A:CU503 4.4 6.0 0.8
HD2 A:HIS65 4.4 6.5 1.0
HD21 A:LEU459 4.5 8.5 1.0
CD2 A:HIS65 4.5 6.4 1.0
CB A:PHE450 4.6 6.5 1.0
NE2 A:HIS65 4.6 6.5 1.0
O2 A:OXY512 4.6 9.6 0.5
CG A:PHE450 4.7 6.9 1.0
HD1 A:HIS452 4.7 8.4 1.0
HE2 A:PHE450 4.7 8.1 1.0
HD1 A:HIS112 4.7 6.7 1.0
HD1 A:HIS402 4.8 6.2 1.0
HB2 A:PHE450 4.8 6.5 1.0
CE2 A:PHE450 4.8 8.2 1.0
NE2 A:HIS400 4.8 6.5 1.0

Copper binding site 3 out of 6 in 5mew

Go back to Copper Binding Sites List in 5mew
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. Second Structure of the Series with Total Exposition Time 33 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. Second Structure of the Series with Total Exposition Time 33 Min. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu502

b:8.1
occ:0.50
 CU A:CU502 0.0 8.1 0.5
CU A:CU502 0.9 5.4 0.4
O A:HOH605 2.0 4.0 0.5
NE2 A:HIS454 2.0 6.9 1.0
O1 A:OXY511 2.1 7.1 0.4
ND1 A:HIS67 2.2 6.5 1.0
O A:HOH605 2.2 6.5 0.5
NE2 A:HIS110 2.2 7.4 1.0
O2 A:OXY511 2.4 7.7 0.4
HD2 A:HIS65 2.9 6.5 1.0
CD2 A:HIS454 3.0 6.5 1.0
CE1 A:HIS110 3.0 7.5 1.0
CE1 A:HIS67 3.0 6.3 1.0
HE1 A:HIS110 3.0 7.3 1.0
CE1 A:HIS454 3.1 6.7 1.0
HE1 A:HIS67 3.1 6.4 1.0
HD2 A:HIS454 3.1 6.5 1.0
HB2 A:HIS67 3.2 5.9 1.0
HE1 A:HIS454 3.3 6.6 1.0
CG A:HIS67 3.3 6.2 1.0
CD2 A:HIS110 3.4 6.9 1.0
HD2 A:HIS400 3.6 6.5 1.0
CU A:CU501 3.6 5.2 0.5
CD2 A:HIS65 3.6 6.4 1.0
CU A:CU503 3.7 6.0 0.8
HD2 A:HIS110 3.7 6.9 1.0
CB A:HIS67 3.8 5.9 1.0
CD2 A:HIS400 3.9 6.6 1.0
NE2 A:HIS400 4.0 6.5 1.0
O A:HOH607 4.1 23.0 0.5
NE2 A:HIS65 4.1 6.5 1.0
HB2 A:ALA244 4.1 5.5 1.0
HE1 A:HIS452 4.1 9.2 1.0
ND1 A:HIS454 4.1 6.3 1.0
CG A:HIS454 4.1 6.1 1.0
HZ2 A:TRP108 4.1 5.8 1.0
NE2 A:HIS67 4.2 6.4 1.0
ND1 A:HIS110 4.2 6.9 1.0
CD2 A:HIS67 4.4 7.0 1.0
O1 A:OXY512 4.4 7.6 0.5
CU A:CU501 4.4 6.2 0.4
HB3 A:HIS67 4.4 5.9 1.0
HD2 A:HIS112 4.4 6.7 1.0
HA A:HIS67 4.4 5.7 1.0
CG A:HIS110 4.5 6.4 1.0
CZ2 A:TRP108 4.5 5.8 1.0
HB1 A:ALA244 4.7 5.5 1.0
HE1 A:TRP108 4.7 5.8 1.0
CG A:HIS400 4.8 6.3 1.0
CA A:HIS67 4.8 5.7 1.0
CE1 A:HIS452 4.8 9.6 1.0
CB A:ALA244 4.8 5.6 1.0
CE2 A:TRP108 4.8 5.6 1.0
NE2 A:HIS452 4.9 9.1 1.0
CG A:HIS65 4.9 6.6 1.0
HD1 A:HIS454 4.9 6.3 1.0
CE1 A:HIS400 4.9 6.7 1.0
HE2 A:HIS67 4.9 6.5 1.0
NE1 A:TRP108 4.9 5.7 1.0
CD2 A:HIS112 4.9 6.8 1.0
NE2 A:HIS112 4.9 6.8 1.0
HD1 A:HIS110 5.0 6.9 1.0

Copper binding site 4 out of 6 in 5mew

Go back to Copper Binding Sites List in 5mew
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. Second Structure of the Series with Total Exposition Time 33 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. Second Structure of the Series with Total Exposition Time 33 Min. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu502

b:5.4
occ:0.40
 CU A:CU502 0.0 5.4 0.4
CU A:CU502 0.9 8.1 0.5
ND1 A:HIS67 1.9 6.5 1.0
NE2 A:HIS110 1.9 7.4 1.0
NE2 A:HIS454 2.1 6.9 1.0
HB2 A:HIS67 2.7 5.9 1.0
CD2 A:HIS110 2.8 6.9 1.0
O A:HOH605 2.9 4.0 0.5
CE1 A:HIS67 2.9 6.3 1.0
CG A:HIS67 2.9 6.2 1.0
HD2 A:HIS110 2.9 6.9 1.0
CE1 A:HIS454 3.0 6.7 1.0
O A:HOH605 3.0 6.5 0.5
CE1 A:HIS110 3.0 7.5 1.0
HE1 A:HIS454 3.0 6.6 1.0
O1 A:OXY511 3.1 7.1 0.4
HE1 A:HIS67 3.1 6.4 1.0
HD2 A:HIS65 3.2 6.5 1.0
O2 A:OXY511 3.2 7.7 0.4
CD2 A:HIS454 3.3 6.5 1.0
CB A:HIS67 3.3 5.9 1.0
HE1 A:HIS110 3.3 7.3 1.0
HZ2 A:TRP108 3.4 5.8 1.0
HD2 A:HIS454 3.5 6.5 1.0
HB2 A:ALA244 3.6 5.5 1.0
CZ2 A:TRP108 3.7 5.8 1.0
HB3 A:HIS67 3.8 5.9 1.0
CE2 A:TRP108 3.9 5.6 1.0
HE1 A:TRP108 3.9 5.8 1.0
NE2 A:HIS67 4.0 6.4 1.0
CD2 A:HIS67 4.0 7.0 1.0
CD2 A:HIS65 4.0 6.4 1.0
CG A:HIS110 4.0 6.4 1.0
NE1 A:TRP108 4.1 5.7 1.0
ND1 A:HIS110 4.1 6.9 1.0
ND1 A:HIS454 4.1 6.3 1.0
CU A:CU503 4.2 6.0 0.8
HB1 A:ALA244 4.3 5.5 1.0
CG A:HIS454 4.3 6.1 1.0
CB A:ALA244 4.4 5.6 1.0
HA A:HIS67 4.4 5.7 1.0
HD2 A:HIS400 4.4 6.5 1.0
CH2 A:TRP108 4.4 5.8 1.0
CA A:HIS67 4.5 5.7 1.0
CU A:CU501 4.5 5.2 0.5
NE2 A:HIS65 4.5 6.5 1.0
NE2 A:HIS400 4.5 6.5 1.0
CD2 A:HIS400 4.5 6.6 1.0
O A:HOH607 4.6 23.0 0.5
HH2 A:TRP108 4.6 5.9 1.0
HE2 A:HIS67 4.7 6.5 1.0
CD2 A:TRP108 4.8 5.4 1.0
HB3 A:ALA244 4.8 5.5 1.0
O1 A:OXY512 4.8 7.6 0.5
HD2 A:HIS67 4.8 6.7 1.0
HD1 A:HIS454 4.9 6.3 1.0
HD1 A:HIS110 4.9 6.9 1.0
HE1 A:HIS452 4.9 9.2 1.0

Copper binding site 5 out of 6 in 5mew

Go back to Copper Binding Sites List in 5mew
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. Second Structure of the Series with Total Exposition Time 33 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. Second Structure of the Series with Total Exposition Time 33 Min. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu503

b:6.0
occ:0.80
 O A:HOH605 1.8 6.5 0.5
NE2 A:HIS65 1.9 6.5 1.0
NE2 A:HIS400 1.9 6.5 1.0
O A:HOH929 2.0 4.8 0.5
O A:HOH1005 2.6 6.1 0.5
CD2 A:HIS400 2.9 6.6 1.0
CE1 A:HIS65 2.9 6.5 1.0
CD2 A:HIS65 2.9 6.4 1.0
CE1 A:HIS400 2.9 6.7 1.0
HA A:HIS67 3.0 5.7 1.0
HD2 A:HIS400 3.1 6.5 1.0
HE1 A:HIS65 3.1 6.5 1.0
HD2 A:HIS65 3.1 6.5 1.0
HE1 A:HIS400 3.2 6.5 1.0
H A:GLY68 3.3 5.6 1.0
O1 A:OXY511 3.3 7.1 0.4
CD2 A:HIS402 3.4 6.1 1.0
ND1 A:HIS67 3.5 6.5 1.0
NE2 A:HIS402 3.5 6.5 1.0
HD2 A:HIS402 3.5 6.1 1.0
HA A:HIS402 3.6 5.9 1.0
CU A:CU502 3.7 8.1 0.5
CG A:HIS402 3.8 5.7 1.0
CG A:HIS67 3.8 6.2 1.0
CU A:CU501 3.8 5.2 0.5
O A:HOH605 3.9 4.0 0.5
CA A:HIS67 3.9 5.7 1.0
CE1 A:HIS402 3.9 6.6 1.0
CE1 A:HIS67 3.9 6.3 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 6.0 1.0
CG A:HIS400 4.0 6.3 1.0
CG A:HIS65 4.0 6.6 1.0
N A:GLY68 4.1 5.6 1.0
HB2 A:HIS67 4.1 5.9 1.0
CB A:HIS67 4.1 5.9 1.0
CU A:CU502 4.2 5.4 0.4
HE1 A:HIS67 4.3 6.4 1.0
CD2 A:HIS67 4.3 7.0 1.0
NE2 A:HIS67 4.4 6.4 1.0
HE1 A:HIS402 4.4 6.5 1.0
CU A:CU501 4.4 6.2 0.4
CA A:HIS402 4.4 5.7 1.0
O2 A:OXY511 4.5 7.7 0.4
C A:HIS67 4.5 5.6 1.0
CB A:HIS402 4.5 6.1 1.0
HD1 A:HIS402 4.6 6.2 1.0
O A:HOH879 4.6 10.4 1.0
O A:HOH710 4.7 9.6 1.0
HB3 A:HIS402 4.8 5.9 1.0
HD1 A:HIS65 4.8 6.5 1.0
HD1 A:HIS400 4.8 6.2 1.0
N A:HIS402 4.8 5.8 1.0
HD2 A:HIS67 4.9 6.7 1.0
HA2 A:GLY68 4.9 5.8 1.0
HE2 A:HIS67 4.9 6.5 1.0
O A:LEU401 4.9 6.2 1.0
HD2 A:HIS112 5.0 6.7 1.0
N A:HIS67 5.0 5.5 1.0

Copper binding site 6 out of 6 in 5mew

Go back to Copper Binding Sites List in 5mew
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. Second Structure of the Series with Total Exposition Time 33 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. Second Structure of the Series with Total Exposition Time 33 Min. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu504

b:6.0
occ:0.90
 ND1 A:HIS397 2.0 6.7 1.0
ND1 A:HIS458 2.0 6.7 1.0
SG A:CYS453 2.2 6.6 1.0
HD11 A:ILE455 2.7 5.9 1.0
CE1 A:HIS397 2.9 7.2 1.0
HD2 A:PHE463 3.0 6.4 1.0
CE1 A:HIS458 3.0 7.4 1.0
CG A:HIS458 3.0 7.0 1.0
HB A:ILE455 3.1 6.3 1.0
CG A:HIS397 3.1 6.2 1.0
HE1 A:HIS397 3.1 7.1 1.0
HB3 A:HIS397 3.1 6.5 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 6.7 1.0
CB A:HIS458 3.4 7.0 1.0
HB2 A:CYS453 3.4 6.5 1.0
HA A:HIS397 3.4 6.3 1.0
HB3 A:CYS453 3.5 6.6 1.0
CB A:HIS397 3.5 6.6 1.0
HE2 A:PHE463 3.5 6.6 1.0
CD1 A:ILE455 3.6 5.8 1.0
CD2 A:PHE463 3.8 6.4 1.0
HD2 A:PRO398 3.8 5.9 1.0
CB A:ILE455 3.9 6.3 1.0
H A:ILE455 3.9 6.4 1.0
CA A:HIS397 4.0 6.4 1.0
HD12 A:ILE455 4.0 5.9 1.0
CE2 A:PHE463 4.1 6.6 1.0
NE2 A:HIS397 4.1 7.2 1.0
NE2 A:HIS458 4.1 7.5 1.0
CG1 A:ILE455 4.1 6.2 1.0
CD2 A:HIS458 4.2 6.8 1.0
CD2 A:HIS397 4.2 7.2 1.0
HD13 A:ILE455 4.2 5.9 1.0
HG13 A:ILE455 4.2 6.1 1.0
HB2 A:HIS397 4.4 6.5 1.0
O A:GLY394 4.6 8.9 1.0
HG21 A:ILE455 4.6 6.4 1.0
HZ A:PHE341 4.6 7.7 1.0
HG22 A:ILE455 4.6 6.4 1.0
CD A:PRO398 4.7 5.9 1.0
CA A:CYS453 4.7 6.2 1.0
CG2 A:ILE455 4.7 6.5 1.0
CZ A:PHE341 4.8 7.8 1.0
HE1 A:PHE399 4.8 7.5 1.0
N A:ILE455 4.8 6.4 1.0
HE2 A:HIS397 4.8 7.2 1.0
HA A:CYS453 4.8 6.3 1.0
HD3 A:PRO398 4.9 5.9 1.0
HE2 A:PHE341 4.9 7.6 1.0
CA A:HIS458 4.9 7.2 1.0
HE2 A:HIS458 4.9 7.3 1.0
CE2 A:PHE341 4.9 7.5 1.0
HB3 A:PHE463 4.9 6.5 1.0
CA A:ILE455 4.9 6.2 1.0
C A:HIS397 5.0 6.1 1.0
O A:ILE455 5.0 6.7 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

Last articles

Zn in 9JPJ
Zn in 9JP7
Zn in 9JPK
Zn in 9JPL
Zn in 9GN6
Zn in 9GN7
Zn in 9GKU
Zn in 9GKW
Zn in 9GKX
Zn in 9GL0
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy