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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

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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

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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

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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

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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

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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

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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

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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

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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

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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

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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: Sat Oct 5 11:56:11 2024

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Zn in 9GKW
Zn in 9GKX
Zn in 9GL0
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