Atomistry » Manganese » PDB 1o9i-1pj3 » 1o9i
Atomistry »
  Manganese »
    PDB 1o9i-1pj3 »
      1o9i »

Manganese in PDB 1o9i: Crystal Structure of the Y42F Mutant of Manganese Catalase From Lactobacillus Plantarum at 1.33A Resolution

Enzymatic activity of Crystal Structure of the Y42F Mutant of Manganese Catalase From Lactobacillus Plantarum at 1.33A Resolution

All present enzymatic activity of Crystal Structure of the Y42F Mutant of Manganese Catalase From Lactobacillus Plantarum at 1.33A Resolution:
1.11.1.6;

Protein crystallography data

The structure of Crystal Structure of the Y42F Mutant of Manganese Catalase From Lactobacillus Plantarum at 1.33A Resolution, PDB code: 1o9i was solved by V.V.Barynin, M.M.Whittaker, J.W.Whittaker, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 50.00 / 1.33
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 73.490, 95.270, 105.000, 90.00, 106.55, 90.00
R / Rfree (%) 11.5 / 14.5

Other elements in 1o9i:

The structure of Crystal Structure of the Y42F Mutant of Manganese Catalase From Lactobacillus Plantarum at 1.33A Resolution also contains other interesting chemical elements:

Calcium (Ca) 6 atoms
Sodium (Na) 2 atoms

Manganese Binding Sites:

Pages:

>>> Page 1 <<< Page 2, Binding sites: 11 - 12;

Binding sites:

The binding sites of Manganese atom in the Crystal Structure of the Y42F Mutant of Manganese Catalase From Lactobacillus Plantarum at 1.33A Resolution (pdb code 1o9i). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 12 binding sites of Manganese where determined in the Crystal Structure of the Y42F Mutant of Manganese Catalase From Lactobacillus Plantarum at 1.33A Resolution, PDB code: 1o9i:
Jump to Manganese binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Manganese binding site 1 out of 12 in 1o9i

Go back to Manganese Binding Sites List in 1o9i
Manganese binding site 1 out of 12 in the Crystal Structure of the Y42F Mutant of Manganese Catalase From Lactobacillus Plantarum at 1.33A Resolution


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Crystal Structure of the Y42F Mutant of Manganese Catalase From Lactobacillus Plantarum at 1.33A Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn267

b:18.2
occ:1.00
OE2 A:GLU35 1.9 18.4 0.6
O A:HOH2228 2.1 21.3 0.4
O A:O270 2.1 22.1 0.8
OE1 A:GLU66 2.1 18.9 1.0
O A:HOH2229 2.1 21.4 0.6
ND1 A:HIS69 2.2 16.8 1.0
OE2 A:GLU35 2.2 16.9 0.4
CD A:GLU35 2.9 18.9 0.6
CE1 A:HIS69 3.1 15.8 1.0
CD A:GLU66 3.1 16.9 1.0
CD A:GLU35 3.2 17.4 0.4
CG A:HIS69 3.3 15.8 1.0
OE1 A:GLU35 3.4 20.9 0.6
OE2 A:GLU66 3.4 18.6 1.0
OE1 A:GLU35 3.4 19.8 0.4
MN A:MN3268 3.5 19.9 1.0
CB A:HIS69 3.7 14.4 1.0
NH2 A:ARG147 4.1 23.9 1.0
CG A:GLU35 4.2 17.1 0.6
NE2 A:HIS69 4.2 15.3 1.0
CD2 A:HIS69 4.4 15.3 1.0
CG A:GLU66 4.5 15.5 1.0
OE2 A:GLU178 4.5 29.0 0.8
CG A:GLU35 4.6 16.9 0.4
CD2 A:LEU174 4.6 19.8 1.0
CA A:GLU66 4.8 13.8 1.0
CG A:GLU178 4.8 20.1 1.0
CB A:GLU35 4.8 15.5 0.6
CB A:GLU66 4.8 14.7 1.0
CE1 A:HIS181 4.9 17.5 1.0
ND1 A:HIS181 4.9 17.1 1.0
CB A:GLU35 4.9 15.3 0.4
OE1 A:GLU148 5.0 16.6 0.6

Manganese binding site 2 out of 12 in 1o9i

Go back to Manganese Binding Sites List in 1o9i
Manganese binding site 2 out of 12 in the Crystal Structure of the Y42F Mutant of Manganese Catalase From Lactobacillus Plantarum at 1.33A Resolution


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Crystal Structure of the Y42F Mutant of Manganese Catalase From Lactobacillus Plantarum at 1.33A Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn268

b:19.9
occ:1.00
OE2 A:GLU66 2.0 18.6 1.0
ND1 A:HIS181 2.1 17.1 1.0
O A:O270 2.1 22.1 0.8
OE2 A:GLU148 2.1 17.0 0.6
OE2 A:GLU148 2.2 17.7 0.4
OE1 A:GLU148 2.3 16.6 0.6
CD A:GLU148 2.5 15.5 0.6
O A:HOH2228 2.9 21.3 0.4
CE1 A:HIS181 2.9 17.5 1.0
CD A:GLU66 3.1 16.9 1.0
CD A:GLU148 3.1 17.3 0.4
CG A:HIS181 3.2 15.8 1.0
NH2 A:ARG147 3.4 23.9 1.0
MN A:MN3267 3.5 18.2 1.0
OE1 A:GLU66 3.5 18.9 1.0
OE1 A:GLU148 3.5 19.5 0.4
CB A:HIS181 3.7 15.0 1.0
CG A:GLU148 4.0 14.1 0.6
NE2 A:HIS181 4.1 16.8 1.0
CD2 A:HIS181 4.3 16.0 1.0
CG A:GLU178 4.4 20.1 1.0
CG A:GLU148 4.4 15.9 0.4
CG A:GLU66 4.4 15.5 1.0
CE2 A:PHE42 4.6 14.6 1.0
O A:HOH2229 4.6 21.4 0.6
CZ A:ARG147 4.6 21.1 1.0
CG2 A:THR62 4.7 14.8 1.0
CA A:GLU178 4.7 16.3 1.0
O A:ARG177 4.8 16.0 1.0
ND1 A:HIS69 4.8 16.8 1.0
CE1 A:HIS69 4.9 15.8 1.0
CB A:GLU148 4.9 14.8 0.4
CB A:GLU148 5.0 14.1 0.6

Manganese binding site 3 out of 12 in 1o9i

Go back to Manganese Binding Sites List in 1o9i
Manganese binding site 3 out of 12 in the Crystal Structure of the Y42F Mutant of Manganese Catalase From Lactobacillus Plantarum at 1.33A Resolution


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 3 of Crystal Structure of the Y42F Mutant of Manganese Catalase From Lactobacillus Plantarum at 1.33A Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mn267

b:18.2
occ:1.00
OE2 B:GLU35 1.9 18.2 0.6
O B:HOH2241 2.1 24.1 0.4
OE1 B:GLU66 2.1 19.1 1.0
ND1 B:HIS69 2.2 16.6 1.0
O B:O270 2.2 23.6 0.7
O B:HOH2242 2.2 22.1 0.6
OE2 B:GLU35 2.2 14.0 0.4
CD B:GLU35 2.9 18.3 0.6
CE1 B:HIS69 3.1 17.1 1.0
CD B:GLU66 3.1 18.2 1.0
CD B:GLU35 3.1 17.4 0.4
CG B:HIS69 3.3 15.8 1.0
OE1 B:GLU35 3.3 20.4 0.4
OE2 B:GLU66 3.4 17.2 1.0
OE1 B:GLU35 3.4 21.5 0.6
MN B:MN3268 3.5 20.0 1.0
CB B:HIS69 3.6 14.4 1.0
NH2 B:ARG147 4.1 21.5 1.0
CG B:GLU35 4.1 17.1 0.6
NE2 B:HIS69 4.2 16.1 1.0
CD2 B:HIS69 4.4 15.6 1.0
OE2 B:GLU178 4.4 28.0 0.8
CG B:GLU66 4.5 15.4 1.0
CG B:GLU35 4.5 16.6 0.4
CD2 B:LEU174 4.7 19.5 1.0
CA B:GLU66 4.7 14.1 1.0
CB B:GLU35 4.8 15.0 0.6
CB B:GLU66 4.8 15.1 1.0
CE1 B:HIS181 4.8 17.3 1.0
CG B:GLU178 4.8 22.1 1.0
ND1 B:HIS181 4.9 18.4 1.0
CB B:GLU35 4.9 14.9 0.4
OE1 B:GLU148 5.0 14.8 0.6

Manganese binding site 4 out of 12 in 1o9i

Go back to Manganese Binding Sites List in 1o9i
Manganese binding site 4 out of 12 in the Crystal Structure of the Y42F Mutant of Manganese Catalase From Lactobacillus Plantarum at 1.33A Resolution


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 4 of Crystal Structure of the Y42F Mutant of Manganese Catalase From Lactobacillus Plantarum at 1.33A Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mn268

b:20.0
occ:1.00
OE2 B:GLU66 2.0 17.2 1.0
ND1 B:HIS181 2.1 18.4 1.0
OE2 B:GLU148 2.1 18.6 0.4
OE2 B:GLU148 2.2 16.4 0.6
O B:O270 2.2 23.6 0.7
OE1 B:GLU148 2.3 14.8 0.6
CD B:GLU148 2.5 15.2 0.6
O B:HOH2241 2.8 24.1 0.4
CE1 B:HIS181 2.9 17.3 1.0
CD B:GLU66 3.1 18.2 1.0
CD B:GLU148 3.1 16.2 0.4
CG B:HIS181 3.2 15.9 1.0
NH2 B:ARG147 3.4 21.5 1.0
OE1 B:GLU66 3.5 19.1 1.0
MN B:MN3267 3.5 18.2 1.0
OE1 B:GLU148 3.5 18.1 0.4
CB B:HIS181 3.7 14.9 1.0
CG B:GLU148 4.0 15.5 0.6
NE2 B:HIS181 4.1 16.9 1.0
CD2 B:HIS181 4.2 16.2 1.0
CG B:GLU178 4.4 22.1 1.0
CG B:GLU148 4.4 16.1 0.4
CG B:GLU66 4.4 15.4 1.0
CE2 B:PHE42 4.5 14.1 1.0
CZ B:ARG147 4.6 20.4 1.0
CG2 B:THR62 4.6 15.6 1.0
O B:HOH2242 4.7 22.1 0.6
CA B:GLU178 4.7 18.3 1.0
O B:ARG177 4.8 15.9 1.0
ND1 B:HIS69 4.9 16.6 1.0
CE1 B:HIS69 4.9 17.1 1.0
CB B:GLU148 5.0 14.2 0.6

Manganese binding site 5 out of 12 in 1o9i

Go back to Manganese Binding Sites List in 1o9i
Manganese binding site 5 out of 12 in the Crystal Structure of the Y42F Mutant of Manganese Catalase From Lactobacillus Plantarum at 1.33A Resolution


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 5 of Crystal Structure of the Y42F Mutant of Manganese Catalase From Lactobacillus Plantarum at 1.33A Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mn267

b:19.8
occ:1.00
OE2 C:GLU35 1.9 18.3 0.6
OE1 C:GLU66 2.1 19.4 1.0
O C:O270 2.1 22.7 0.7
O C:HOH2241 2.1 22.2 0.4
O C:HOH2242 2.2 23.9 0.6
ND1 C:HIS69 2.2 17.6 1.0
OE2 C:GLU35 2.3 15.7 0.4
CD C:GLU35 2.9 19.3 0.6
CE1 C:HIS69 3.1 17.7 1.0
CD C:GLU66 3.1 18.0 1.0
CD C:GLU35 3.2 17.2 0.4
CG C:HIS69 3.3 16.2 1.0
OE1 C:GLU35 3.3 22.6 0.6
OE1 C:GLU35 3.4 19.8 0.4
OE2 C:GLU66 3.4 20.8 1.0
MN C:MN3268 3.5 21.5 1.0
CB C:HIS69 3.7 15.4 1.0
NH2 C:ARG147 4.1 22.1 1.0
CG C:GLU35 4.1 17.9 0.6
NE2 C:HIS69 4.2 16.8 1.0
CD2 C:HIS69 4.4 16.7 1.0
CG C:GLU66 4.4 17.3 1.0
OE2 C:GLU178 4.5 28.4 0.7
CD2 C:LEU174 4.6 20.9 1.0
CG C:GLU35 4.6 17.4 0.4
CA C:GLU66 4.7 15.0 1.0
CB C:GLU35 4.8 16.0 0.6
CB C:GLU66 4.8 15.3 1.0
CG C:GLU178 4.8 21.7 1.0
ND1 C:HIS181 4.9 19.5 1.0
CE1 C:HIS181 4.9 17.6 1.0
CB C:GLU35 4.9 15.9 0.4

Manganese binding site 6 out of 12 in 1o9i

Go back to Manganese Binding Sites List in 1o9i
Manganese binding site 6 out of 12 in the Crystal Structure of the Y42F Mutant of Manganese Catalase From Lactobacillus Plantarum at 1.33A Resolution


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 6 of Crystal Structure of the Y42F Mutant of Manganese Catalase From Lactobacillus Plantarum at 1.33A Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mn268

b:21.5
occ:1.00
OE2 C:GLU66 2.0 20.8 1.0
O C:O270 2.1 22.7 0.7
ND1 C:HIS181 2.1 19.5 1.0
OE1 C:GLU148 2.1 16.0 0.5
OE2 C:GLU148 2.2 18.1 0.6
OE1 C:GLU148 2.3 15.2 0.6
CD C:GLU148 2.6 15.2 0.6
O C:HOH2241 2.6 22.2 0.4
CE1 C:HIS181 3.0 17.6 1.0
CD C:GLU148 3.1 15.8 0.5
CD C:GLU66 3.1 18.0 1.0
CG C:HIS181 3.2 15.7 1.0
NH2 C:ARG147 3.5 22.1 1.0
OE2 C:GLU148 3.5 17.5 0.5
OE1 C:GLU66 3.5 19.4 1.0
MN C:MN3267 3.5 19.8 1.0
CB C:HIS181 3.7 16.1 1.0
CG C:GLU148 4.0 15.5 0.6
NE2 C:HIS181 4.1 18.1 1.0
CD2 C:HIS181 4.3 17.6 1.0
CG C:GLU148 4.3 16.5 0.5
CG C:GLU178 4.3 21.7 1.0
CG C:GLU66 4.4 17.3 1.0
CE2 C:PHE42 4.6 16.2 1.0
CG2 C:THR62 4.6 15.7 1.0
CZ C:ARG147 4.7 21.9 1.0
O C:HOH2242 4.7 23.9 0.6
CA C:GLU178 4.7 17.1 1.0
O C:ARG177 4.7 17.3 1.0
ND1 C:HIS69 4.9 17.6 1.0
CE1 C:HIS69 4.9 17.7 1.0
CB C:GLU148 5.0 15.4 0.5
CB C:GLU148 5.0 15.2 0.6

Manganese binding site 7 out of 12 in 1o9i

Go back to Manganese Binding Sites List in 1o9i
Manganese binding site 7 out of 12 in the Crystal Structure of the Y42F Mutant of Manganese Catalase From Lactobacillus Plantarum at 1.33A Resolution


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 7 of Crystal Structure of the Y42F Mutant of Manganese Catalase From Lactobacillus Plantarum at 1.33A Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Mn267

b:18.7
occ:1.00
OE2 D:GLU35 1.9 18.7 0.6
O D:HOH2243 2.0 23.3 0.4
O D:O270 2.1 23.6 0.8
OE1 D:GLU66 2.1 19.2 1.0
O D:HOH2242 2.2 24.1 0.6
ND1 D:HIS69 2.2 16.7 1.0
OE2 D:GLU35 2.2 16.8 0.5
CD D:GLU35 2.9 18.4 0.6
CD D:GLU66 3.1 18.0 1.0
CE1 D:HIS69 3.1 16.0 1.0
CD D:GLU35 3.1 18.1 0.5
CG D:HIS69 3.3 15.6 1.0
OE1 D:GLU35 3.3 22.2 0.6
OE1 D:GLU35 3.4 20.3 0.5
OE2 D:GLU66 3.4 20.6 1.0
MN D:MN3268 3.5 20.3 1.0
CB D:HIS69 3.7 15.0 1.0
NH2 D:ARG147 4.0 22.4 1.0
CG D:GLU35 4.1 16.0 0.6
NE2 D:HIS69 4.2 16.2 1.0
CD2 D:HIS69 4.3 15.8 1.0
CG D:GLU66 4.4 15.7 1.0
OE2 D:GLU178 4.5 29.5 0.8
CG D:GLU35 4.5 17.5 0.5
CD2 D:LEU174 4.6 19.0 1.0
CA D:GLU66 4.7 14.1 1.0
CB D:GLU35 4.8 15.0 0.6
CG D:GLU178 4.8 20.4 1.0
CB D:GLU66 4.8 14.4 1.0
CE1 D:HIS181 4.9 17.7 1.0
ND1 D:HIS181 4.9 17.6 1.0
CB D:GLU35 4.9 15.3 0.5
OE1 D:GLU148 5.0 17.3 0.6

Manganese binding site 8 out of 12 in 1o9i

Go back to Manganese Binding Sites List in 1o9i
Manganese binding site 8 out of 12 in the Crystal Structure of the Y42F Mutant of Manganese Catalase From Lactobacillus Plantarum at 1.33A Resolution


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 8 of Crystal Structure of the Y42F Mutant of Manganese Catalase From Lactobacillus Plantarum at 1.33A Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Mn268

b:20.3
occ:1.00
OE2 D:GLU66 2.0 20.6 1.0
ND1 D:HIS181 2.1 17.6 1.0
OE2 D:GLU148 2.1 16.7 0.6
O D:O270 2.2 23.6 0.8
OE1 D:GLU148 2.2 17.0 0.4
OE1 D:GLU148 2.3 17.3 0.6
CD D:GLU148 2.5 16.4 0.6
O D:HOH2243 2.6 23.3 0.4
CE1 D:HIS181 2.9 17.7 1.0
CD D:GLU66 3.1 18.0 1.0
CD D:GLU148 3.1 15.5 0.4
CG D:HIS181 3.2 16.2 1.0
NH2 D:ARG147 3.4 22.4 1.0
MN D:MN3267 3.5 18.7 1.0
OE2 D:GLU148 3.5 16.6 0.4
OE1 D:GLU66 3.5 19.2 1.0
CB D:HIS181 3.6 15.8 1.0
CG D:GLU148 4.0 14.4 0.6
NE2 D:HIS181 4.1 17.4 1.0
CD2 D:HIS181 4.2 17.5 1.0
CG D:GLU148 4.4 14.7 0.4
CG D:GLU178 4.4 20.4 1.0
CG D:GLU66 4.4 15.7 1.0
CG2 D:THR62 4.6 15.3 1.0
CE2 D:PHE42 4.6 14.1 1.0
CZ D:ARG147 4.7 20.5 1.0
O D:ARG177 4.7 16.7 1.0
CA D:GLU178 4.7 16.6 1.0
O D:HOH2242 4.7 24.1 0.6
ND1 D:HIS69 4.9 16.7 1.0
CE1 D:HIS69 4.9 16.0 1.0
CB D:GLU148 4.9 14.6 0.4
CB D:GLU148 5.0 14.6 0.6

Manganese binding site 9 out of 12 in 1o9i

Go back to Manganese Binding Sites List in 1o9i
Manganese binding site 9 out of 12 in the Crystal Structure of the Y42F Mutant of Manganese Catalase From Lactobacillus Plantarum at 1.33A Resolution


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 9 of Crystal Structure of the Y42F Mutant of Manganese Catalase From Lactobacillus Plantarum at 1.33A Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Mn267

b:19.7
occ:1.00
O E:HOH2245 1.8 21.8 0.4
OE2 E:GLU35 1.9 20.2 0.6
O E:O270 2.1 22.8 0.8
OE1 E:GLU66 2.1 20.2 1.0
ND1 E:HIS69 2.2 17.4 1.0
O E:HOH2246 2.2 21.8 0.6
OE2 E:GLU35 2.2 16.3 0.5
CD E:GLU35 2.9 19.6 0.6
CD E:GLU66 3.1 18.9 1.0
CE1 E:HIS69 3.1 16.1 1.0
CD E:GLU35 3.2 18.3 0.5
CG E:HIS69 3.3 15.6 1.0
OE2 E:GLU66 3.4 19.9 1.0
OE1 E:GLU35 3.4 21.2 0.6
MN E:MN3268 3.5 21.1 1.0
OE1 E:GLU35 3.5 20.6 0.5
CB E:HIS69 3.6 15.1 1.0
NH2 E:ARG147 4.1 23.9 1.0
CG E:GLU35 4.1 16.4 0.6
NE2 E:HIS69 4.2 16.3 1.0
CD2 E:HIS69 4.3 17.0 1.0
CG E:GLU66 4.4 16.3 1.0
OE2 E:GLU178 4.5 30.6 1.0
CG E:GLU35 4.6 17.4 0.5
CD2 E:LEU174 4.7 19.5 1.0
CB E:GLU35 4.7 15.8 0.6
CA E:GLU66 4.7 15.5 1.0
CG E:GLU178 4.8 21.5 1.0
CB E:GLU66 4.8 15.5 1.0
CE1 E:HIS181 4.9 18.1 1.0
ND1 E:HIS181 4.9 18.3 1.0
CB E:GLU35 4.9 16.2 0.5
OE1 E:GLU148 5.0 18.1 0.7

Manganese binding site 10 out of 12 in 1o9i

Go back to Manganese Binding Sites List in 1o9i
Manganese binding site 10 out of 12 in the Crystal Structure of the Y42F Mutant of Manganese Catalase From Lactobacillus Plantarum at 1.33A Resolution


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 10 of Crystal Structure of the Y42F Mutant of Manganese Catalase From Lactobacillus Plantarum at 1.33A Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Mn268

b:21.1
occ:1.00
OE2 E:GLU66 2.0 19.9 1.0
ND1 E:HIS181 2.1 18.3 1.0
OE2 E:GLU148 2.1 17.9 0.7
OE2 E:GLU148 2.1 14.6 0.3
O E:O270 2.1 22.8 0.8
OE1 E:GLU148 2.3 18.1 0.7
O E:HOH2245 2.3 21.8 0.4
CD E:GLU148 2.5 18.2 0.7
CE1 E:HIS181 2.9 18.1 1.0
CD E:GLU66 3.1 18.9 1.0
CD E:GLU148 3.1 13.8 0.3
CG E:HIS181 3.2 16.5 1.0
MN E:MN3267 3.5 19.7 1.0
OE1 E:GLU66 3.5 20.2 1.0
OE1 E:GLU148 3.5 14.1 0.3
NH2 E:ARG147 3.5 23.9 1.0
CB E:HIS181 3.6 16.0 1.0
CG E:GLU148 4.0 16.4 0.7
NE2 E:HIS181 4.1 19.1 1.0
CD2 E:HIS181 4.2 17.8 1.0
CG E:GLU178 4.4 21.5 1.0
CG E:GLU148 4.4 14.5 0.3
CG E:GLU66 4.4 16.3 1.0
CE2 E:PHE42 4.6 15.1 1.0
CG2 E:THR62 4.6 17.7 1.0
CA E:GLU178 4.7 17.1 1.0
O E:ARG177 4.7 17.1 1.0
O E:HOH2246 4.7 21.8 0.6
CZ E:ARG147 4.7 20.5 1.0
ND1 E:HIS69 4.9 17.4 1.0
CE1 E:HIS69 4.9 16.1 1.0
CB E:GLU148 4.9 14.8 0.7
CB E:GLU148 5.0 14.6 0.3

Reference:

M.M.Whittaker, V.V.Barynin, T.Igarashi, J.W.Whittaker. Outer Sphere Mutagenesis of Lactobacillus Plantarum Manganese Catalase Disrupts the Cluster Core. Mechanistic Implications. Eur.J.Biochem. V. 270 1102 2003.
ISSN: ISSN 0014-2956
PubMed: 12631270
DOI: 10.1046/J.1432-1033.2003.03459.X
Page generated: Tue Dec 15 03:53:41 2020

Last articles

Zn in 7VD8
Zn in 7V1R
Zn in 7V1Q
Zn in 7VPF
Zn in 7T85
Zn in 7T5F
Zn in 7NF9
Zn in 7M4M
Zn in 7M4O
Zn in 7M4N
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy