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Magnesium in PDB 3wqp: Crystal Structure of Rubisco T289D Mutant From Thermococcus Kodakarensis

Enzymatic activity of Crystal Structure of Rubisco T289D Mutant From Thermococcus Kodakarensis

All present enzymatic activity of Crystal Structure of Rubisco T289D Mutant From Thermococcus Kodakarensis:
4.1.1.39;

Protein crystallography data

The structure of Crystal Structure of Rubisco T289D Mutant From Thermococcus Kodakarensis, PDB code: 3wqp was solved by M.Fujihashi, Y.Nishitani, T.Kiriyama, K.Miki, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 50.00 / 2.25
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 170.566, 246.238, 144.628, 90.00, 90.00, 90.00
R / Rfree (%) 22 / 25.8

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of Rubisco T289D Mutant From Thermococcus Kodakarensis (pdb code 3wqp). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 10 binding sites of Magnesium where determined in the Crystal Structure of Rubisco T289D Mutant From Thermococcus Kodakarensis, PDB code: 3wqp:
Jump to Magnesium binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Magnesium binding site 1 out of 10 in 3wqp

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Magnesium binding site 1 out of 10 in the Crystal Structure of Rubisco T289D Mutant From Thermococcus Kodakarensis


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure of Rubisco T289D Mutant From Thermococcus Kodakarensis within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg501

b:36.1
occ:1.00
OD1 A:ASP191 2.0 34.9 1.0
OQ2 A:KCX189 2.0 34.5 1.0
OE1 A:GLU192 2.1 33.9 1.0
O7 A:CAP502 2.2 37.1 1.0
O3 A:CAP502 2.3 37.5 1.0
O2 A:CAP502 2.5 38.4 1.0
C A:CAP502 3.0 38.3 1.0
CG A:ASP191 3.0 34.8 1.0
C2 A:CAP502 3.1 38.9 1.0
CX A:KCX189 3.1 35.3 1.0
CD A:GLU192 3.2 33.5 1.0
C3 A:CAP502 3.2 38.6 1.0
OQ1 A:KCX189 3.3 36.0 1.0
N A:GLU192 3.6 32.6 1.0
OE2 A:GLU192 3.7 33.7 1.0
OD2 A:ASP191 3.7 35.6 1.0
NZ A:LYS165 3.8 34.5 1.0
CA A:ASP191 3.9 33.5 1.0
NE2 A:HIS281 4.1 34.1 1.0
CB A:ASP191 4.1 34.1 1.0
NZ A:LYS163 4.1 36.5 1.0
O6 A:CAP502 4.2 38.8 1.0
NZ A:KCX189 4.3 35.1 1.0
C A:ASP191 4.3 32.6 1.0
CG A:GLU192 4.4 32.8 1.0
CG1 A:VAL161 4.4 36.5 1.0
C4 A:CAP502 4.4 39.1 1.0
CB A:GLU192 4.5 32.5 1.0
C1 A:CAP502 4.5 40.2 1.0
CA A:GLU192 4.6 32.2 1.0
CG2 A:VAL161 4.6 37.1 1.0
CD2 A:HIS281 4.7 34.0 1.0
CE1 A:HIS281 4.9 33.9 1.0
C5 A:CAP502 5.0 38.7 1.0
O1 A:CAP502 5.0 40.9 1.0
CB A:VAL161 5.0 37.4 1.0
O A:HOH783 5.0 32.0 1.0

Magnesium binding site 2 out of 10 in 3wqp

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Magnesium binding site 2 out of 10 in the Crystal Structure of Rubisco T289D Mutant From Thermococcus Kodakarensis


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Crystal Structure of Rubisco T289D Mutant From Thermococcus Kodakarensis within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg501

b:59.4
occ:1.00
OE1 B:GLU192 1.9 50.8 1.0
OD1 B:ASP191 2.1 53.0 1.0
OQ2 B:KCX189 2.2 50.5 1.0
O3 B:CAP502 2.3 57.3 1.0
O7 B:CAP502 2.3 60.0 1.0
O2 B:CAP502 2.5 59.4 1.0
CD B:GLU192 3.0 50.7 1.0
CG B:ASP191 3.1 53.4 1.0
C B:CAP502 3.1 61.0 1.0
C2 B:CAP502 3.1 60.3 1.0
C3 B:CAP502 3.3 58.7 1.0
CX B:KCX189 3.3 50.4 1.0
OE2 B:GLU192 3.5 52.1 1.0
N B:GLU192 3.6 48.7 1.0
OQ1 B:KCX189 3.7 51.1 1.0
NZ B:LYS165 3.7 55.6 1.0
OD2 B:ASP191 3.7 55.1 1.0
NE2 B:HIS281 3.9 48.8 1.0
CA B:ASP191 4.0 50.4 1.0
CB B:ASP191 4.1 52.0 1.0
NZ B:LYS163 4.1 57.3 1.0
CG B:GLU192 4.2 48.9 1.0
O6 B:CAP502 4.3 62.4 1.0
C B:ASP191 4.3 49.1 1.0
CB B:GLU192 4.4 47.7 1.0
NZ B:KCX189 4.5 49.1 1.0
C4 B:CAP502 4.5 59.1 1.0
CG1 B:VAL161 4.6 53.1 1.0
C1 B:CAP502 4.6 61.6 1.0
CA B:GLU192 4.6 47.4 1.0
CE1 B:HIS281 4.6 48.4 1.0
CD2 B:HIS281 4.7 47.8 1.0
CE B:LYS165 5.0 56.1 1.0

Magnesium binding site 3 out of 10 in 3wqp

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Magnesium binding site 3 out of 10 in the Crystal Structure of Rubisco T289D Mutant From Thermococcus Kodakarensis


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Crystal Structure of Rubisco T289D Mutant From Thermococcus Kodakarensis within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mg501

b:46.3
occ:1.00
OE1 C:GLU192 1.8 41.3 1.0
OD1 C:ASP191 1.9 43.9 1.0
OQ2 C:KCX189 2.1 42.1 1.0
O7 C:CAP502 2.2 47.0 1.0
O3 C:CAP502 2.4 45.1 1.0
O2 C:CAP502 2.7 47.2 1.0
CD C:GLU192 2.8 41.3 1.0
CG C:ASP191 3.0 44.4 1.0
C C:CAP502 3.1 47.7 1.0
C2 C:CAP502 3.2 47.5 1.0
CX C:KCX189 3.2 41.4 1.0
OE2 C:GLU192 3.3 42.3 1.0
C3 C:CAP502 3.4 46.2 1.0
N C:GLU192 3.4 40.3 1.0
OQ1 C:KCX189 3.6 41.6 1.0
NZ C:LYS165 3.6 45.6 1.0
OD2 C:ASP191 3.6 45.9 1.0
NE2 C:HIS281 3.8 40.4 1.0
CA C:ASP191 3.9 42.1 1.0
CB C:ASP191 4.0 43.7 1.0
CG C:GLU192 4.1 40.0 1.0
C C:ASP191 4.2 40.8 1.0
CB C:GLU192 4.2 39.1 1.0
O6 C:CAP502 4.3 48.8 1.0
NZ C:LYS163 4.3 48.2 1.0
NZ C:KCX189 4.3 40.6 1.0
CA C:GLU192 4.4 39.4 1.0
C4 C:CAP502 4.5 46.3 1.0
CE1 C:HIS281 4.5 40.0 1.0
CD2 C:HIS281 4.6 39.7 1.0
C1 C:CAP502 4.7 48.6 1.0
CG1 C:VAL161 4.8 45.2 1.0
C5 C:CAP502 5.0 45.1 1.0

Magnesium binding site 4 out of 10 in 3wqp

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Magnesium binding site 4 out of 10 in the Crystal Structure of Rubisco T289D Mutant From Thermococcus Kodakarensis


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 4 of Crystal Structure of Rubisco T289D Mutant From Thermococcus Kodakarensis within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Mg501

b:31.5
occ:1.00
OQ2 D:KCX189 1.9 30.4 1.0
OD1 D:ASP191 2.0 30.0 1.0
O7 D:CAP502 2.1 32.7 1.0
OE1 D:GLU192 2.1 29.3 1.0
O3 D:CAP502 2.2 33.4 1.0
O2 D:CAP502 2.5 34.2 1.0
C D:CAP502 2.9 33.8 1.0
C2 D:CAP502 3.0 34.6 1.0
CX D:KCX189 3.0 30.8 1.0
CG D:ASP191 3.1 30.0 1.0
C3 D:CAP502 3.1 34.7 1.0
CD D:GLU192 3.2 28.8 1.0
OQ1 D:KCX189 3.3 31.6 1.0
OE2 D:GLU192 3.6 28.8 1.0
NZ D:LYS163 3.7 32.1 1.0
OD2 D:ASP191 3.7 30.6 1.0
NZ D:LYS165 3.8 29.8 1.0
N D:GLU192 3.8 28.3 1.0
CA D:ASP191 4.0 29.1 1.0
O6 D:CAP502 4.0 34.2 1.0
NE2 D:HIS281 4.1 32.3 1.0
CB D:ASP191 4.1 29.3 1.0
NZ D:KCX189 4.2 30.7 1.0
CG1 D:VAL161 4.3 31.5 1.0
C4 D:CAP502 4.4 35.7 1.0
C D:ASP191 4.4 28.3 1.0
CG D:GLU192 4.4 28.2 1.0
C1 D:CAP502 4.5 35.9 1.0
CG2 D:VAL161 4.6 32.2 1.0
CB D:GLU192 4.7 28.0 1.0
CD2 D:HIS281 4.8 32.1 1.0
CA D:GLU192 4.8 27.8 1.0
C5 D:CAP502 4.9 35.6 1.0
CB D:VAL161 4.9 32.5 1.0
CE D:LYS163 4.9 33.1 1.0
CE1 D:HIS281 4.9 31.8 1.0
O1 D:CAP502 4.9 35.9 1.0

Magnesium binding site 5 out of 10 in 3wqp

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Magnesium binding site 5 out of 10 in the Crystal Structure of Rubisco T289D Mutant From Thermococcus Kodakarensis


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 5 of Crystal Structure of Rubisco T289D Mutant From Thermococcus Kodakarensis within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Mg501

b:45.6
occ:1.00
O7 E:CAP502 2.0 51.7 1.0
OE1 E:GLU192 2.0 40.6 1.0
OD1 E:ASP191 2.1 44.6 1.0
OQ2 E:KCX189 2.3 41.2 1.0
O3 E:CAP502 2.4 48.3 1.0
O2 E:CAP502 2.5 51.9 1.0
C E:CAP502 2.9 52.8 1.0
C2 E:CAP502 3.1 52.1 1.0
CG E:ASP191 3.1 44.0 1.0
CD E:GLU192 3.1 40.5 1.0
C3 E:CAP502 3.3 50.1 1.0
CX E:KCX189 3.4 40.6 1.0
OE2 E:GLU192 3.6 41.8 1.0
OD2 E:ASP191 3.6 44.7 1.0
OQ1 E:KCX189 3.6 41.0 1.0
NZ E:LYS165 3.8 44.1 1.0
N E:GLU192 3.9 39.5 1.0
NE2 E:HIS281 4.0 38.6 1.0
NZ E:LYS163 4.1 47.7 1.0
O6 E:CAP502 4.1 54.4 1.0
CA E:ASP191 4.2 41.3 1.0
CB E:ASP191 4.2 43.1 1.0
CG E:GLU192 4.4 39.1 1.0
C4 E:CAP502 4.4 50.3 1.0
C1 E:CAP502 4.5 53.6 1.0
NZ E:KCX189 4.5 39.5 1.0
C E:ASP191 4.6 40.0 1.0
CB E:GLU192 4.6 38.2 1.0
CG1 E:VAL161 4.6 45.0 1.0
CD2 E:HIS281 4.7 37.9 1.0
CE1 E:HIS281 4.8 38.1 1.0
C5 E:CAP502 4.8 48.6 1.0
CA E:GLU192 4.8 38.5 1.0
O1 E:CAP502 5.0 55.2 1.0

Magnesium binding site 6 out of 10 in 3wqp

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Magnesium binding site 6 out of 10 in the Crystal Structure of Rubisco T289D Mutant From Thermococcus Kodakarensis


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 6 of Crystal Structure of Rubisco T289D Mutant From Thermococcus Kodakarensis within 5.0Å range:
probe atom residue distance (Å) B Occ
F:Mg501

b:46.1
occ:1.00
OQ2 F:KCX189 1.9 44.4 1.0
OD1 F:ASP191 2.0 44.8 1.0
OE1 F:GLU192 2.1 44.1 1.0
O7 F:CAP502 2.4 50.0 1.0
O2 F:CAP502 2.5 51.0 1.0
O3 F:CAP502 2.5 49.3 1.0
CG F:ASP191 3.0 44.3 1.0
CD F:GLU192 3.1 43.3 1.0
CX F:KCX189 3.1 44.6 1.0
C2 F:CAP502 3.1 51.9 1.0
C F:CAP502 3.1 51.4 1.0
C3 F:CAP502 3.4 51.5 1.0
OQ1 F:KCX189 3.5 46.5 1.0
OE2 F:GLU192 3.5 43.6 1.0
N F:GLU192 3.6 40.9 1.0
OD2 F:ASP191 3.7 45.5 1.0
NZ F:LYS165 3.8 45.1 1.0
CA F:ASP191 3.8 41.6 1.0
CB F:ASP191 4.0 42.5 1.0
NE2 F:HIS281 4.1 45.0 1.0
NZ F:LYS163 4.1 49.2 1.0
NZ F:KCX189 4.2 43.6 1.0
C F:ASP191 4.3 40.5 1.0
CG F:GLU192 4.3 42.2 1.0
O6 F:CAP502 4.4 52.8 1.0
CG1 F:VAL161 4.4 45.5 1.0
CB F:GLU192 4.5 41.2 1.0
C1 F:CAP502 4.6 53.8 1.0
C4 F:CAP502 4.6 52.7 1.0
CA F:GLU192 4.7 40.2 1.0
CD2 F:HIS281 4.8 44.4 1.0
CG2 F:VAL161 4.8 46.4 1.0
CE1 F:HIS281 4.9 44.4 1.0
O F:HOH770 4.9 37.1 1.0
O1 F:CAP502 5.0 54.3 1.0

Magnesium binding site 7 out of 10 in 3wqp

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Magnesium binding site 7 out of 10 in the Crystal Structure of Rubisco T289D Mutant From Thermococcus Kodakarensis


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 7 of Crystal Structure of Rubisco T289D Mutant From Thermococcus Kodakarensis within 5.0Å range:
probe atom residue distance (Å) B Occ
G:Mg501

b:57.5
occ:1.00
OE1 G:GLU192 2.0 49.9 1.0
OQ2 G:KCX189 2.0 49.5 1.0
O3 G:CAP502 2.3 54.1 1.0
OD2 G:ASP191 2.3 52.1 1.0
O7 G:CAP502 2.4 56.0 1.0
O2 G:CAP502 2.5 56.5 1.0
CD G:GLU192 3.1 49.4 1.0
CG G:ASP191 3.1 52.6 1.0
C2 G:CAP502 3.2 56.9 1.0
C G:CAP502 3.2 56.9 1.0
CX G:KCX189 3.2 49.4 1.0
C3 G:CAP502 3.3 55.3 1.0
OQ1 G:KCX189 3.6 49.6 1.0
OD1 G:ASP191 3.6 54.3 1.0
N G:GLU192 3.6 48.4 1.0
OE2 G:GLU192 3.6 50.3 1.0
NZ G:LYS165 3.6 52.7 1.0
CA G:ASP191 3.9 50.2 1.0
NZ G:LYS163 4.0 55.1 1.0
NE2 G:HIS281 4.0 47.7 1.0
CB G:ASP191 4.1 51.6 1.0
C G:ASP191 4.3 48.8 1.0
CG G:GLU192 4.3 47.9 1.0
NZ G:KCX189 4.3 48.6 1.0
O6 G:CAP502 4.4 57.4 1.0
CB G:GLU192 4.4 47.2 1.0
CG1 G:VAL161 4.4 53.3 1.0
C4 G:CAP502 4.5 55.3 1.0
CA G:GLU192 4.6 47.3 1.0
C1 G:CAP502 4.6 58.3 1.0
CD2 G:HIS281 4.7 47.2 1.0
CE1 G:HIS281 4.7 47.2 1.0
CG2 G:VAL161 4.9 52.2 1.0
CE G:LYS165 4.9 53.0 1.0

Magnesium binding site 8 out of 10 in 3wqp

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Magnesium binding site 8 out of 10 in the Crystal Structure of Rubisco T289D Mutant From Thermococcus Kodakarensis


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 8 of Crystal Structure of Rubisco T289D Mutant From Thermococcus Kodakarensis within 5.0Å range:
probe atom residue distance (Å) B Occ
H:Mg501

b:58.1
occ:1.00
OE1 H:GLU192 2.0 51.2 1.0
OQ2 H:KCX189 2.0 51.8 1.0
O7 H:CAP502 2.1 60.3 1.0
OD2 H:ASP191 2.3 53.4 1.0
O3 H:CAP502 2.4 58.1 1.0
O2 H:CAP502 2.8 60.9 1.0
CG H:ASP191 3.0 53.6 1.0
C H:CAP502 3.0 61.8 1.0
CD H:GLU192 3.1 51.0 1.0
CX H:KCX189 3.2 51.2 1.0
C2 H:CAP502 3.3 61.6 1.0
OD1 H:ASP191 3.3 55.3 1.0
C3 H:CAP502 3.4 59.8 1.0
N H:GLU192 3.6 48.5 1.0
OQ1 H:KCX189 3.6 52.2 1.0
OE2 H:GLU192 3.6 52.6 1.0
NZ H:LYS165 3.7 54.4 1.0
CA H:ASP191 3.9 50.1 1.0
NE2 H:HIS281 4.0 49.8 1.0
CB H:ASP191 4.0 52.1 1.0
NZ H:LYS163 4.1 57.4 1.0
O6 H:CAP502 4.2 63.3 1.0
C H:ASP191 4.3 48.7 1.0
NZ H:KCX189 4.3 49.7 1.0
CG H:GLU192 4.3 49.1 1.0
CG1 H:VAL161 4.4 53.8 1.0
CB H:GLU192 4.4 47.6 1.0
C4 H:CAP502 4.6 60.2 1.0
CA H:GLU192 4.6 47.2 1.0
CD2 H:HIS281 4.7 48.5 1.0
CE1 H:HIS281 4.7 49.2 1.0
C1 H:CAP502 4.8 63.6 1.0
CG2 H:VAL161 4.9 53.0 1.0
C5 H:CAP502 5.0 58.5 1.0

Magnesium binding site 9 out of 10 in 3wqp

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Magnesium binding site 9 out of 10 in the Crystal Structure of Rubisco T289D Mutant From Thermococcus Kodakarensis


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 9 of Crystal Structure of Rubisco T289D Mutant From Thermococcus Kodakarensis within 5.0Å range:
probe atom residue distance (Å) B Occ
I:Mg501

b:28.2
occ:1.00
OD1 I:ASP191 1.9 27.4 1.0
OQ2 I:KCX189 2.0 27.2 1.0
OE1 I:GLU192 2.1 26.8 1.0
O7 I:CAP502 2.1 31.8 1.0
O3 I:CAP502 2.3 31.1 1.0
O2 I:CAP502 2.3 32.4 1.0
C I:CAP502 2.9 32.2 1.0
C2 I:CAP502 2.9 32.7 1.0
CG I:ASP191 3.0 27.4 1.0
CD I:GLU192 3.1 26.4 1.0
C3 I:CAP502 3.2 32.3 1.0
CX I:KCX189 3.2 27.2 1.0
OQ1 I:KCX189 3.5 27.7 1.0
OE2 I:GLU192 3.6 26.8 1.0
NZ I:LYS163 3.6 30.4 1.0
OD2 I:ASP191 3.6 28.1 1.0
NZ I:LYS165 3.6 30.6 1.0
N I:GLU192 3.9 25.8 1.0
CA I:ASP191 4.1 26.5 1.0
NE2 I:HIS281 4.1 28.2 1.0
CB I:ASP191 4.1 27.0 1.0
O6 I:CAP502 4.1 32.9 1.0
NZ I:KCX189 4.2 27.0 1.0
C4 I:CAP502 4.4 32.8 1.0
C1 I:CAP502 4.4 33.7 1.0
CG I:GLU192 4.4 25.8 1.0
CG1 I:VAL161 4.5 28.0 1.0
C I:ASP191 4.5 25.9 1.0
CB I:GLU192 4.6 25.5 1.0
O I:HOH673 4.8 24.1 1.0
CD2 I:HIS281 4.8 28.1 1.0
O1 I:CAP502 4.9 34.0 1.0
CA I:GLU192 4.9 25.4 1.0
CE1 I:HIS281 4.9 27.6 1.0
CE I:LYS163 4.9 31.2 1.0
C5 I:CAP502 4.9 32.6 1.0
CG2 I:VAL161 4.9 28.5 1.0

Magnesium binding site 10 out of 10 in 3wqp

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Magnesium binding site 10 out of 10 in the Crystal Structure of Rubisco T289D Mutant From Thermococcus Kodakarensis


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 10 of Crystal Structure of Rubisco T289D Mutant From Thermococcus Kodakarensis within 5.0Å range:
probe atom residue distance (Å) B Occ
J:Mg501

b:43.9
occ:1.00
O7 J:CAP502 1.9 48.3 1.0
OQ2 J:KCX189 2.1 39.7 1.0
OE1 J:GLU192 2.1 37.3 1.0
O3 J:CAP502 2.4 45.5 1.0
O2 J:CAP502 2.7 48.8 1.0
C J:CAP502 2.8 49.1 1.0
OD1 J:ASP191 2.8 40.3 1.0
C2 J:CAP502 3.1 48.8 1.0
CG J:ASP191 3.1 40.7 1.0
CD J:GLU192 3.1 37.4 1.0
OD2 J:ASP191 3.2 42.1 1.0
CX J:KCX189 3.2 39.2 1.0
C3 J:CAP502 3.3 46.9 1.0
OE2 J:GLU192 3.5 38.4 1.0
OQ1 J:KCX189 3.5 39.6 1.0
NZ J:LYS163 3.8 44.9 1.0
NZ J:LYS165 3.8 42.0 1.0
N J:GLU192 3.9 36.8 1.0
O6 J:CAP502 4.0 50.4 1.0
CA J:ASP191 4.0 38.6 1.0
CB J:ASP191 4.2 40.0 1.0
NE2 J:HIS281 4.2 34.6 1.0
NZ J:KCX189 4.4 38.3 1.0
CG1 J:VAL161 4.4 41.5 1.0
CG J:GLU192 4.5 36.2 1.0
C J:ASP191 4.5 37.3 1.0
C4 J:CAP502 4.5 46.5 1.0
C1 J:CAP502 4.6 50.0 1.0
CB J:GLU192 4.7 35.5 1.0
CG2 J:VAL161 4.8 40.9 1.0
O J:HOH854 4.8 41.4 1.0
CA J:GLU192 4.9 35.9 1.0
CD2 J:HIS281 4.9 34.1 1.0
O1 J:CAP502 4.9 51.7 1.0
CE1 J:HIS281 5.0 34.3 1.0
C5 J:CAP502 5.0 44.6 1.0

Reference:

T.Kiriyama, M.Fujihashi, Y.Nishitani, R.Aono, T.Sato, T.Takai, K.Tagashira, W.Fukuda, H.Atomi, T.Imanaka, K.Miki. Mutation Design of Thermophilic Rubisco Based on the Three-Dimensional Structure Enhances Its Activity at Ambient Temperature To Be Published.
Page generated: Mon Dec 14 09:01:39 2020

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