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Magnesium in PDB 3a12: Crystal Structure of Type III Rubisco Complexed with 2-Cabp

Enzymatic activity of Crystal Structure of Type III Rubisco Complexed with 2-Cabp

All present enzymatic activity of Crystal Structure of Type III Rubisco Complexed with 2-Cabp:
4.1.1.39;

Protein crystallography data

The structure of Crystal Structure of Type III Rubisco Complexed with 2-Cabp, PDB code: 3a12 was solved by Y.Nishitani, M.Fujihashi, T.Doi, S.Yoshida, H.Atomi, T.Imanaka, K.Miki, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 35.39 / 2.30
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 173.287, 246.377, 144.589, 90.00, 90.00, 90.00
R / Rfree (%) 19.9 / 24.4

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of Type III Rubisco Complexed with 2-Cabp (pdb code 3a12). 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 Type III Rubisco Complexed with 2-Cabp, PDB code: 3a12:
Jump to Magnesium binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Magnesium binding site 1 out of 10 in 3a12

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Magnesium binding site 1 out of 10 in the Crystal Structure of Type III Rubisco Complexed with 2-Cabp


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 Type III Rubisco Complexed with 2-Cabp within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg445

b:15.6
occ:1.00
O7 A:CAP446 1.9 18.1 1.0
OE1 A:GLU192 2.0 18.3 1.0
OQ2 A:KCX189 2.0 17.1 1.0
OD1 A:ASP191 2.0 15.7 1.0
O3 A:CAP446 2.1 19.1 1.0
O2 A:CAP446 2.4 18.5 1.0
C A:CAP446 2.7 18.7 1.0
C2 A:CAP446 2.8 19.1 1.0
CD A:GLU192 2.9 16.5 1.0
C3 A:CAP446 3.0 19.0 1.0
CX A:KCX189 3.1 16.6 1.0
CG A:ASP191 3.2 16.6 1.0
OE2 A:GLU192 3.2 17.3 1.0
OQ1 A:KCX189 3.4 18.8 1.0
NZ A:LYS165 3.7 19.6 1.0
N A:GLU192 3.8 14.4 1.0
O6 A:CAP446 3.9 18.4 1.0
NZ A:LYS163 4.0 20.4 1.0
OD2 A:ASP191 4.0 20.3 1.0
NE2 A:HIS281 4.0 12.4 1.0
CA A:ASP191 4.1 15.0 1.0
C4 A:CAP446 4.2 19.5 1.0
NZ A:KCX189 4.2 15.1 1.0
CB A:ASP191 4.3 15.2 1.0
CG A:GLU192 4.3 16.4 1.0
C1 A:CAP446 4.3 18.8 1.0
C A:ASP191 4.5 14.4 1.0
CB A:GLU192 4.6 14.9 1.0
CG1 A:VAL161 4.6 19.1 1.0
CD2 A:HIS281 4.8 13.4 1.0
C5 A:CAP446 4.8 17.6 1.0
O1 A:CAP446 4.8 20.0 1.0
O A:HOH615 4.8 37.7 1.0
CA A:GLU192 4.8 14.8 1.0
CE1 A:HIS281 4.8 12.9 1.0
CG2 A:VAL161 4.9 18.3 1.0

Magnesium binding site 2 out of 10 in 3a12

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Magnesium binding site 2 out of 10 in the Crystal Structure of Type III Rubisco Complexed with 2-Cabp


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 Type III Rubisco Complexed with 2-Cabp within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg445

b:17.3
occ:1.00
OD1 B:ASP191 2.0 16.4 1.0
OQ2 B:KCX189 2.0 15.7 1.0
O7 B:CAP446 2.0 20.6 1.0
OE1 B:GLU192 2.0 13.4 1.0
O3 B:CAP446 2.1 19.8 1.0
O2 B:CAP446 2.2 20.6 1.0
C B:CAP446 2.7 20.6 1.0
C2 B:CAP446 2.7 21.0 1.0
C3 B:CAP446 2.9 20.1 1.0
CX B:KCX189 3.0 13.2 1.0
CD B:GLU192 3.1 12.6 1.0
CG B:ASP191 3.1 14.9 1.0
OQ1 B:KCX189 3.2 13.3 1.0
OE2 B:GLU192 3.5 14.8 1.0
NZ B:LYS163 3.8 17.4 1.0
OD2 B:ASP191 3.8 19.4 1.0
NZ B:LYS165 3.9 17.7 1.0
N B:GLU192 3.9 13.1 1.0
O6 B:CAP446 3.9 20.4 1.0
NE2 B:HIS281 4.0 12.5 1.0
C4 B:CAP446 4.2 19.8 1.0
CA B:ASP191 4.2 13.3 1.0
NZ B:KCX189 4.2 12.3 1.0
C1 B:CAP446 4.2 20.1 1.0
CB B:ASP191 4.3 13.0 1.0
CG B:GLU192 4.4 12.7 1.0
CG1 B:VAL161 4.5 16.0 1.0
CB B:GLU192 4.6 13.2 1.0
C B:ASP191 4.6 13.2 1.0
O1 B:CAP446 4.7 20.0 1.0
C5 B:CAP446 4.7 18.3 1.0
CE1 B:HIS281 4.8 13.0 1.0
CD2 B:HIS281 4.9 12.3 1.0
CA B:GLU192 4.9 13.4 1.0
CG2 B:VAL161 4.9 16.1 1.0

Magnesium binding site 3 out of 10 in 3a12

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Magnesium binding site 3 out of 10 in the Crystal Structure of Type III Rubisco Complexed with 2-Cabp


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 Type III Rubisco Complexed with 2-Cabp within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mg445

b:21.7
occ:1.00
O7 C:CAP446 1.8 20.2 1.0
OD1 C:ASP191 1.9 19.6 1.0
OQ2 C:KCX189 1.9 18.0 1.0
OE1 C:GLU192 2.1 18.8 1.0
O3 C:CAP446 2.1 22.4 1.0
O2 C:CAP446 2.4 21.3 1.0
C C:CAP446 2.6 21.3 1.0
C2 C:CAP446 2.7 22.0 1.0
C3 C:CAP446 2.9 21.9 1.0
CX C:KCX189 3.0 17.3 1.0
CG C:ASP191 3.2 18.7 1.0
CD C:GLU192 3.2 18.4 1.0
OQ1 C:KCX189 3.2 18.6 1.0
OE2 C:GLU192 3.7 20.4 1.0
O6 C:CAP446 3.8 21.8 1.0
NZ C:LYS163 3.9 24.7 1.0
OD2 C:ASP191 3.9 22.9 1.0
NZ C:LYS165 3.9 21.5 1.0
N C:GLU192 3.9 16.9 1.0
NE2 C:HIS281 4.1 11.5 1.0
CA C:ASP191 4.1 16.8 1.0
C4 C:CAP446 4.1 22.7 1.0
NZ C:KCX189 4.1 14.6 1.0
CB C:ASP191 4.2 17.1 1.0
C1 C:CAP446 4.2 21.2 1.0
CG C:GLU192 4.5 16.9 1.0
CG1 C:VAL161 4.5 19.1 1.0
C C:ASP191 4.6 17.0 1.0
CB C:GLU192 4.6 17.1 1.0
O1 C:CAP446 4.7 22.6 1.0
CD2 C:HIS281 4.8 12.6 1.0
C5 C:CAP446 4.8 22.1 1.0
CG2 C:VAL161 4.8 18.5 1.0
CA C:GLU192 4.9 17.0 1.0
CE1 C:HIS281 4.9 13.5 1.0

Magnesium binding site 4 out of 10 in 3a12

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Magnesium binding site 4 out of 10 in the Crystal Structure of Type III Rubisco Complexed with 2-Cabp


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 Type III Rubisco Complexed with 2-Cabp within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Mg445

b:12.0
occ:1.00
OD1 D:ASP191 1.9 16.6 1.0
OQ2 D:KCX189 1.9 11.2 1.0
O3 D:CAP446 2.1 16.2 1.0
OE1 D:GLU192 2.1 14.2 1.0
O7 D:CAP446 2.2 14.2 1.0
O2 D:CAP446 2.3 14.4 1.0
C2 D:CAP446 2.8 15.1 1.0
C D:CAP446 2.8 14.8 1.0
CX D:KCX189 2.9 10.4 1.0
C3 D:CAP446 2.9 15.9 1.0
CG D:ASP191 3.1 15.1 1.0
OQ1 D:KCX189 3.2 11.0 1.0
CD D:GLU192 3.2 15.3 1.0
OE2 D:GLU192 3.7 14.6 1.0
NZ D:LYS163 3.8 16.8 1.0
OD2 D:ASP191 3.8 19.5 1.0
N D:GLU192 3.8 13.1 1.0
NE2 D:HIS281 4.0 12.2 1.0
NZ D:LYS165 4.0 15.9 1.0
O6 D:CAP446 4.1 14.5 1.0
CA D:ASP191 4.1 13.7 1.0
NZ D:KCX189 4.1 10.1 1.0
CB D:ASP191 4.2 13.6 1.0
C4 D:CAP446 4.2 16.9 1.0
C1 D:CAP446 4.3 14.9 1.0
CG1 D:VAL161 4.4 14.6 1.0
C D:ASP191 4.5 13.5 1.0
CG D:GLU192 4.5 13.7 1.0
CB D:GLU192 4.7 13.3 1.0
O1 D:CAP446 4.7 15.9 1.0
CD2 D:HIS281 4.8 11.9 1.0
C5 D:CAP446 4.8 16.0 1.0
CE1 D:HIS281 4.8 13.4 1.0
CG2 D:VAL161 4.8 15.7 1.0
CA D:GLU192 4.9 13.4 1.0

Magnesium binding site 5 out of 10 in 3a12

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Magnesium binding site 5 out of 10 in the Crystal Structure of Type III Rubisco Complexed with 2-Cabp


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 Type III Rubisco Complexed with 2-Cabp within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Mg445

b:25.2
occ:1.00
O7 E:CAP446 1.8 29.5 1.0
O3 E:CAP446 2.0 28.9 1.0
OQ2 E:KCX189 2.1 18.3 1.0
OE1 E:GLU192 2.2 20.4 1.0
O2 E:CAP446 2.2 29.8 1.0
OD2 E:ASP191 2.3 24.8 1.0
C E:CAP446 2.5 29.9 1.0
C2 E:CAP446 2.6 29.8 1.0
C3 E:CAP446 2.8 28.8 1.0
CX E:KCX189 3.1 18.0 1.0
CD E:GLU192 3.2 20.4 1.0
CG E:ASP191 3.3 22.3 1.0
OQ1 E:KCX189 3.3 19.8 1.0
OE2 E:GLU192 3.5 22.0 1.0
O6 E:CAP446 3.7 30.7 1.0
NZ E:LYS163 3.7 22.2 1.0
OD1 E:ASP191 3.9 26.1 1.0
NZ E:LYS165 4.0 21.6 1.0
C4 E:CAP446 4.0 28.0 1.0
N E:GLU192 4.0 18.8 1.0
NE2 E:HIS281 4.0 14.1 1.0
C1 E:CAP446 4.1 29.9 1.0
NZ E:KCX189 4.2 16.0 1.0
CA E:ASP191 4.2 19.4 1.0
CB E:ASP191 4.4 20.0 1.0
CG1 E:VAL161 4.5 19.4 1.0
CG E:GLU192 4.6 19.4 1.0
O1 E:CAP446 4.6 30.5 1.0
C5 E:CAP446 4.6 27.1 1.0
C E:ASP191 4.7 19.0 1.0
CE1 E:HIS281 4.8 15.1 1.0
CB E:GLU192 4.8 18.9 1.0
CG2 E:VAL161 4.9 19.5 1.0
CE E:LYS163 4.9 23.4 1.0
CD2 E:HIS281 4.9 14.5 1.0

Magnesium binding site 6 out of 10 in 3a12

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Magnesium binding site 6 out of 10 in the Crystal Structure of Type III Rubisco Complexed with 2-Cabp


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 Type III Rubisco Complexed with 2-Cabp within 5.0Å range:
probe atom residue distance (Å) B Occ
F:Mg445

b:21.1
occ:1.00
OQ2 F:KCX189 1.7 26.9 1.0
OE1 F:GLU192 2.0 22.4 1.0
OD1 F:ASP191 2.0 22.8 1.0
O7 F:CAP446 2.2 25.5 1.0
O3 F:CAP446 2.2 25.0 1.0
O2 F:CAP446 2.4 24.7 1.0
CX F:KCX189 2.8 27.0 1.0
C2 F:CAP446 2.9 25.2 1.0
C F:CAP446 2.9 25.0 1.0
C3 F:CAP446 3.0 24.8 1.0
CG F:ASP191 3.1 20.9 1.0
CD F:GLU192 3.1 22.1 1.0
OQ1 F:KCX189 3.2 28.1 1.0
OE2 F:GLU192 3.6 21.4 1.0
N F:GLU192 3.6 19.6 1.0
OD2 F:ASP191 3.8 24.1 1.0
CA F:ASP191 3.9 20.1 1.0
NZ F:KCX189 3.9 25.6 1.0
NE2 F:HIS281 4.0 13.2 1.0
NZ F:LYS163 4.1 22.7 1.0
CB F:ASP191 4.1 20.1 1.0
O6 F:CAP446 4.1 24.0 1.0
NZ F:LYS165 4.2 27.6 1.0
C F:ASP191 4.3 19.8 1.0
C4 F:CAP446 4.3 23.9 1.0
CG F:GLU192 4.4 20.9 1.0
C1 F:CAP446 4.4 24.8 1.0
CG1 F:VAL161 4.4 24.0 1.0
CE F:LYS165 4.4 26.3 1.0
CB F:GLU192 4.5 19.5 1.0
CA F:GLU192 4.6 19.7 1.0
CD2 F:HIS281 4.7 15.6 1.0
CG2 F:VAL161 4.8 22.8 1.0
CE1 F:HIS281 4.9 15.9 1.0
C5 F:CAP446 4.9 21.4 1.0
O1 F:CAP446 4.9 24.7 1.0

Magnesium binding site 7 out of 10 in 3a12

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Magnesium binding site 7 out of 10 in the Crystal Structure of Type III Rubisco Complexed with 2-Cabp


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 Type III Rubisco Complexed with 2-Cabp within 5.0Å range:
probe atom residue distance (Å) B Occ
G:Mg445

b:26.9
occ:1.00
OE1 G:GLU192 2.1 16.2 1.0
OQ2 G:KCX189 2.1 21.2 1.0
O7 G:CAP446 2.1 25.5 1.0
O3 G:CAP446 2.2 25.4 1.0
O2 G:CAP446 2.3 25.0 1.0
OD2 G:ASP191 2.4 26.6 1.0
C G:CAP446 2.8 25.5 1.0
C2 G:CAP446 2.8 25.5 1.0
C3 G:CAP446 3.0 25.3 1.0
CG G:ASP191 3.1 24.0 1.0
CX G:KCX189 3.1 21.8 1.0
CD G:GLU192 3.1 18.5 1.0
OQ1 G:KCX189 3.4 23.1 1.0
OD1 G:ASP191 3.4 28.9 1.0
OE2 G:GLU192 3.6 19.3 1.0
NZ G:LYS165 3.7 24.4 1.0
N G:GLU192 3.8 20.2 1.0
NZ G:LYS163 3.9 24.4 1.0
O6 G:CAP446 4.0 25.7 1.0
CA G:ASP191 4.1 21.4 1.0
NE2 G:HIS281 4.1 16.5 1.0
CB G:ASP191 4.2 21.9 1.0
C4 G:CAP446 4.2 25.7 1.0
NZ G:KCX189 4.3 21.5 1.0
C1 G:CAP446 4.3 25.4 1.0
CG G:GLU192 4.4 18.6 1.0
CG1 G:VAL161 4.4 22.6 1.0
C G:ASP191 4.5 20.9 1.0
CB G:GLU192 4.6 19.4 1.0
O1 G:CAP446 4.7 26.1 1.0
CA G:GLU192 4.8 19.6 1.0
C5 G:CAP446 4.9 24.5 1.0
CD2 G:HIS281 4.9 16.8 1.0
CE1 G:HIS281 4.9 17.1 1.0
CG2 G:VAL161 4.9 22.9 1.0

Magnesium binding site 8 out of 10 in 3a12

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Magnesium binding site 8 out of 10 in the Crystal Structure of Type III Rubisco Complexed with 2-Cabp


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 Type III Rubisco Complexed with 2-Cabp within 5.0Å range:
probe atom residue distance (Å) B Occ
H:Mg445

b:27.1
occ:1.00
O7 H:CAP446 2.0 28.6 1.0
OE1 H:GLU192 2.1 22.7 1.0
OQ2 H:KCX189 2.2 24.0 1.0
O3 H:CAP446 2.3 27.6 1.0
O2 H:CAP446 2.4 29.7 1.0
OD2 H:ASP191 2.7 25.9 1.0
C H:CAP446 2.7 29.0 1.0
C2 H:CAP446 2.9 29.2 1.0
OD1 H:ASP191 2.9 28.8 1.0
CG H:ASP191 3.0 25.1 1.0
CD H:GLU192 3.1 23.0 1.0
C3 H:CAP446 3.1 28.9 1.0
CX H:KCX189 3.3 22.1 1.0
NZ H:LYS165 3.4 29.0 1.0
OE2 H:GLU192 3.4 24.8 1.0
NZ H:LYS163 3.6 25.8 1.0
OQ1 H:KCX189 3.6 22.4 1.0
N H:GLU192 3.9 22.7 1.0
O6 H:CAP446 3.9 28.9 1.0
CA H:ASP191 4.1 23.3 1.0
CB H:ASP191 4.1 23.8 1.0
NE2 H:HIS281 4.3 19.6 1.0
C4 H:CAP446 4.4 29.2 1.0
C1 H:CAP446 4.4 29.5 1.0
CG H:GLU192 4.4 22.6 1.0
NZ H:KCX189 4.4 21.2 1.0
C H:ASP191 4.5 22.9 1.0
CG1 H:VAL161 4.7 26.4 1.0
CB H:GLU192 4.7 22.5 1.0
CE H:LYS165 4.8 28.7 1.0
O1 H:CAP446 4.9 31.0 1.0
CA H:GLU192 4.9 22.3 1.0
C5 H:CAP446 4.9 28.6 1.0
CE H:LYS163 4.9 26.9 1.0

Magnesium binding site 9 out of 10 in 3a12

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Magnesium binding site 9 out of 10 in the Crystal Structure of Type III Rubisco Complexed with 2-Cabp


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 Type III Rubisco Complexed with 2-Cabp within 5.0Å range:
probe atom residue distance (Å) B Occ
I:Mg445

b:11.6
occ:1.00
OQ2 I:KCX189 1.9 12.8 1.0
OD1 I:ASP191 2.0 13.2 1.0
OE1 I:GLU192 2.0 14.5 1.0
O7 I:CAP446 2.1 15.2 1.0
O3 I:CAP446 2.1 18.2 1.0
O2 I:CAP446 2.3 14.7 1.0
C I:CAP446 2.8 15.3 1.0
C2 I:CAP446 2.8 15.6 1.0
C3 I:CAP446 3.0 15.7 1.0
CX I:KCX189 3.0 12.8 1.0
CD I:GLU192 3.1 15.1 1.0
CG I:ASP191 3.2 12.8 1.0
OQ1 I:KCX189 3.3 13.4 1.0
OE2 I:GLU192 3.5 16.9 1.0
N I:GLU192 3.8 11.7 1.0
NZ I:LYS163 3.8 15.2 1.0
OD2 I:ASP191 3.9 18.1 1.0
NZ I:LYS165 4.0 19.3 1.0
CA I:ASP191 4.0 12.1 1.0
O6 I:CAP446 4.0 14.6 1.0
NE2 I:HIS281 4.1 12.3 1.0
C4 I:CAP446 4.2 16.8 1.0
NZ I:KCX189 4.2 11.3 1.0
CB I:ASP191 4.2 12.1 1.0
C1 I:CAP446 4.3 14.7 1.0
CG I:GLU192 4.4 13.2 1.0
C I:ASP191 4.4 11.9 1.0
CG1 I:VAL161 4.5 13.0 1.0
CB I:GLU192 4.6 11.8 1.0
C5 I:CAP446 4.8 14.9 1.0
O1 I:CAP446 4.8 13.9 1.0
CE1 I:HIS281 4.8 11.8 1.0
CA I:GLU192 4.8 12.1 1.0
CD2 I:HIS281 4.9 12.2 1.0
CG2 I:VAL161 5.0 13.4 1.0

Magnesium binding site 10 out of 10 in 3a12

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Magnesium binding site 10 out of 10 in the Crystal Structure of Type III Rubisco Complexed with 2-Cabp


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 Type III Rubisco Complexed with 2-Cabp within 5.0Å range:
probe atom residue distance (Å) B Occ
J:Mg445

b:16.4
occ:1.00
O7 J:CAP446 1.7 27.3 1.0
OE1 J:GLU192 2.0 17.4 1.0
O3 J:CAP446 2.1 25.6 1.0
OQ2 J:KCX189 2.1 20.7 1.0
OD1 J:ASP191 2.2 24.9 1.0
O2 J:CAP446 2.3 27.9 1.0
C J:CAP446 2.5 27.7 1.0
C2 J:CAP446 2.6 27.6 1.0
C3 J:CAP446 2.9 26.6 1.0
CD J:GLU192 3.0 17.8 1.0
CX J:KCX189 3.1 20.6 1.0
CG J:ASP191 3.3 22.8 1.0
OE2 J:GLU192 3.3 19.2 1.0
OQ1 J:KCX189 3.4 22.2 1.0
O6 J:CAP446 3.6 28.4 1.0
NZ J:LYS163 3.7 23.3 1.0
N J:GLU192 3.9 18.7 1.0
OD2 J:ASP191 3.9 26.6 1.0
C4 J:CAP446 4.1 26.1 1.0
NE2 J:HIS281 4.1 15.8 1.0
C1 J:CAP446 4.1 27.1 1.0
CA J:ASP191 4.2 19.6 1.0
NZ J:KCX189 4.3 19.4 1.0
CE J:LYS165 4.3 23.7 1.0
CB J:ASP191 4.3 20.2 1.0
CG J:GLU192 4.3 18.3 1.0
NZ J:LYS165 4.4 25.0 1.0
C J:ASP191 4.6 19.2 1.0
CB J:GLU192 4.6 18.5 1.0
CG1 J:VAL161 4.6 21.9 1.0
O1 J:CAP446 4.6 27.5 1.0
C5 J:CAP446 4.7 25.1 1.0
CA J:GLU192 4.8 18.8 1.0
CE1 J:HIS281 4.9 15.8 1.0
CD2 J:HIS281 4.9 16.0 1.0
CG2 J:VAL161 5.0 21.9 1.0
CE J:LYS163 5.0 24.5 1.0

Reference:

Y.Nishitani, S.Yoshida, M.Fujihashi, K.Kitagawa, T.Doi, H.Atomi, T.Imanaka, K.Miki. Structure-Based Catalytic Optimization of A Type III Rubisco From A Hyperthermophile J.Biol.Chem. V. 285 39339 2010.
ISSN: ISSN 0021-9258
PubMed: 20926376
DOI: 10.1074/JBC.M110.147587
Page generated: Mon Dec 14 07:52:14 2020

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