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Magnesium in PDB 2v69: Crystal Structure of Chlamydomonas Reinhardtii Rubisco with A Large- Subunit Mutation D473E

Enzymatic activity of Crystal Structure of Chlamydomonas Reinhardtii Rubisco with A Large- Subunit Mutation D473E

All present enzymatic activity of Crystal Structure of Chlamydomonas Reinhardtii Rubisco with A Large- Subunit Mutation D473E:
4.1.1.39;

Protein crystallography data

The structure of Crystal Structure of Chlamydomonas Reinhardtii Rubisco with A Large- Subunit Mutation D473E, PDB code: 2v69 was solved by S.Karkehabadi, S.Satagopan, T.C.Taylor, R.J.Spreitzer, I.Andersson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 2.80
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 114.242, 169.140, 137.179, 90.00, 96.24, 90.00
R / Rfree (%) 19.7 / 22.8

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of Chlamydomonas Reinhardtii Rubisco with A Large- Subunit Mutation D473E (pdb code 2v69). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 8 binding sites of Magnesium where determined in the Crystal Structure of Chlamydomonas Reinhardtii Rubisco with A Large- Subunit Mutation D473E, PDB code: 2v69:
Jump to Magnesium binding site number: 1; 2; 3; 4; 5; 6; 7; 8;

Magnesium binding site 1 out of 8 in 2v69

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Magnesium binding site 1 out of 8 in the Crystal Structure of Chlamydomonas Reinhardtii Rubisco with A Large- Subunit Mutation D473E


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 Chlamydomonas Reinhardtii Rubisco with A Large- Subunit Mutation D473E within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1470

b:47.4
occ:1.00
OQ1 A:KCX201 1.9 53.1 1.0
OD1 A:ASP203 1.9 50.1 1.0
OE1 A:GLU204 2.0 49.7 1.0
O3 A:CAP1471 2.2 53.5 1.0
O2 A:CAP1471 2.3 56.0 1.0
O7 A:CAP1471 2.3 56.9 1.0
C2 A:CAP1471 2.9 56.1 1.0
C A:CAP1471 3.0 56.4 1.0
CX A:KCX201 3.0 52.2 1.0
CG A:ASP203 3.1 48.9 1.0
C3 A:CAP1471 3.1 55.5 1.0
CD A:GLU204 3.1 49.8 1.0
OQ2 A:KCX201 3.5 53.4 1.0
NZ A:LYS177 3.6 46.4 1.0
OE2 A:GLU204 3.6 50.6 1.0
N A:GLU204 3.7 46.2 1.0
OD2 A:ASP203 3.8 51.4 1.0
CG2 A:THR173 3.9 49.4 1.0
NE2 A:HIS294 4.0 45.4 1.0
ND2 B:ASN123 4.0 51.2 1.0
CA A:ASP203 4.0 46.7 1.0
NZ A:LYS175 4.1 45.0 1.0
NZ A:KCX201 4.1 49.9 1.0
CB A:ASP203 4.1 47.1 1.0
O6 A:CAP1471 4.2 56.8 1.0
CG A:GLU204 4.3 47.6 1.0
C A:ASP203 4.4 46.4 1.0
C4 A:CAP1471 4.4 55.3 1.0
C1 A:CAP1471 4.4 56.1 1.0
CB A:GLU204 4.4 46.1 1.0
OG1 A:THR173 4.4 49.6 1.0
CD2 A:HIS294 4.6 44.2 1.0
CA A:GLU204 4.7 45.9 1.0
CB A:THR173 4.7 49.2 1.0
C5 A:CAP1471 4.8 54.9 1.0
O1 A:CAP1471 4.9 54.5 1.0
CE1 A:HIS294 4.9 44.0 1.0
CE A:LYS177 5.0 45.9 1.0

Magnesium binding site 2 out of 8 in 2v69

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Magnesium binding site 2 out of 8 in the Crystal Structure of Chlamydomonas Reinhardtii Rubisco with A Large- Subunit Mutation D473E


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 Chlamydomonas Reinhardtii Rubisco with A Large- Subunit Mutation D473E within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg1470

b:47.8
occ:1.00
OQ1 B:KCX201 2.0 53.5 1.0
OD1 B:ASP203 2.0 50.0 1.0
OE1 B:GLU204 2.1 49.5 1.0
O7 B:CAP1471 2.2 56.7 1.0
O3 B:CAP1471 2.3 53.7 1.0
O2 B:CAP1471 2.3 55.5 1.0
C B:CAP1471 2.9 56.4 1.0
C2 B:CAP1471 2.9 56.0 1.0
CG B:ASP203 3.0 49.5 1.0
CD B:GLU204 3.1 49.8 1.0
C3 B:CAP1471 3.1 55.7 1.0
CX B:KCX201 3.1 52.8 1.0
OE2 B:GLU204 3.6 51.1 1.0
OQ2 B:KCX201 3.6 54.1 1.0
OD2 B:ASP203 3.6 52.2 1.0
NZ B:LYS177 3.6 46.9 1.0
N B:GLU204 3.7 46.3 1.0
CG2 B:THR173 3.9 49.4 1.0
NZ B:LYS175 3.9 45.2 1.0
ND2 A:ASN123 4.0 51.0 1.0
NE2 B:HIS294 4.0 46.4 1.0
CA B:ASP203 4.1 47.0 1.0
O6 B:CAP1471 4.1 56.8 1.0
CB B:ASP203 4.1 47.5 1.0
NZ B:KCX201 4.2 50.5 1.0
CG B:GLU204 4.3 47.6 1.0
C1 B:CAP1471 4.4 56.1 1.0
C B:ASP203 4.4 46.6 1.0
C4 B:CAP1471 4.4 56.0 1.0
CB B:GLU204 4.5 46.3 1.0
OG1 B:THR173 4.6 49.5 1.0
CD2 B:HIS294 4.6 44.5 1.0
CA B:GLU204 4.7 46.1 1.0
CB B:THR173 4.7 49.4 1.0
C5 B:CAP1471 4.9 55.0 1.0
O1 B:CAP1471 4.9 55.2 1.0
CE B:LYS177 4.9 46.0 1.0
CE1 B:HIS294 5.0 44.1 1.0

Magnesium binding site 3 out of 8 in 2v69

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Magnesium binding site 3 out of 8 in the Crystal Structure of Chlamydomonas Reinhardtii Rubisco with A Large- Subunit Mutation D473E


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 Chlamydomonas Reinhardtii Rubisco with A Large- Subunit Mutation D473E within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mg1471

b:46.1
occ:1.00
OQ1 C:KCX201 1.8 53.4 1.0
OD1 C:ASP203 1.9 49.6 1.0
OE1 C:GLU204 2.1 49.5 1.0
O3 C:CAP1472 2.2 53.8 1.0
O2 C:CAP1472 2.3 56.2 1.0
O7 C:CAP1472 2.3 56.5 1.0
CX C:KCX201 3.0 52.2 1.0
C2 C:CAP1472 3.0 56.0 1.0
C C:CAP1472 3.0 56.2 1.0
CG C:ASP203 3.0 48.3 1.0
CD C:GLU204 3.1 49.9 1.0
C3 C:CAP1472 3.2 55.3 1.0
OQ2 C:KCX201 3.5 53.3 1.0
NZ C:LYS177 3.6 46.4 1.0
OE2 C:GLU204 3.7 50.1 1.0
N C:GLU204 3.7 45.9 1.0
OD2 C:ASP203 3.7 51.2 1.0
ND2 D:ASN123 4.0 50.9 1.0
NZ C:KCX201 4.0 49.5 1.0
CG2 C:THR173 4.0 48.6 1.0
NE2 C:HIS294 4.0 45.1 1.0
CA C:ASP203 4.0 46.4 1.0
CB C:ASP203 4.1 46.8 1.0
NZ C:LYS175 4.1 44.5 1.0
O6 C:CAP1472 4.2 56.6 1.0
CG C:GLU204 4.3 47.9 1.0
OG1 C:THR173 4.3 49.4 1.0
C C:ASP203 4.4 46.0 1.0
CB C:GLU204 4.4 46.0 1.0
C4 C:CAP1472 4.4 54.7 1.0
C1 C:CAP1472 4.4 55.8 1.0
CD2 C:HIS294 4.6 44.3 1.0
CA C:GLU204 4.7 45.5 1.0
CB C:THR173 4.7 49.1 1.0
C5 C:CAP1472 4.8 54.5 1.0
CE1 C:HIS294 4.9 44.1 1.0
O1 C:CAP1472 5.0 54.2 1.0

Magnesium binding site 4 out of 8 in 2v69

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Magnesium binding site 4 out of 8 in the Crystal Structure of Chlamydomonas Reinhardtii Rubisco with A Large- Subunit Mutation D473E


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 Chlamydomonas Reinhardtii Rubisco with A Large- Subunit Mutation D473E within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Mg1475

b:48.0
occ:1.00
OD1 D:ASP203 1.8 50.0 1.0
OQ1 D:KCX201 2.0 52.8 1.0
OE1 D:GLU204 2.0 49.7 1.0
O7 D:CAP1476 2.3 56.7 1.0
O2 D:CAP1476 2.3 55.4 1.0
O3 D:CAP1476 2.4 53.5 1.0
CG D:ASP203 3.0 48.7 1.0
C2 D:CAP1476 3.0 55.9 1.0
C D:CAP1476 3.0 56.1 1.0
CX D:KCX201 3.0 52.1 1.0
CD D:GLU204 3.1 49.9 1.0
C3 D:CAP1476 3.2 55.2 1.0
OQ2 D:KCX201 3.5 53.8 1.0
NZ D:LYS177 3.5 46.4 1.0
OE2 D:GLU204 3.5 50.8 1.0
N D:GLU204 3.6 46.2 1.0
OD2 D:ASP203 3.7 51.4 1.0
CA D:ASP203 3.9 46.8 1.0
CG2 D:THR173 3.9 49.7 1.0
CB D:ASP203 4.0 47.0 1.0
NE2 D:HIS294 4.0 45.0 1.0
ND2 C:ASN123 4.1 51.0 1.0
NZ D:KCX201 4.1 49.7 1.0
NZ D:LYS175 4.2 45.1 1.0
O6 D:CAP1476 4.2 56.5 1.0
C D:ASP203 4.3 46.5 1.0
CG D:GLU204 4.3 47.4 1.0
C4 D:CAP1476 4.4 54.7 1.0
OG1 D:THR173 4.5 49.6 1.0
C1 D:CAP1476 4.5 56.2 1.0
CB D:GLU204 4.5 46.1 1.0
CD2 D:HIS294 4.5 44.4 1.0
CA D:GLU204 4.6 46.0 1.0
CB D:THR173 4.8 49.1 1.0
C5 D:CAP1476 4.9 54.5 1.0
CE D:LYS177 4.9 46.0 1.0
O C:HOH1015 4.9 43.0 1.0
O1 D:CAP1476 5.0 55.0 1.0
CE1 D:HIS294 5.0 43.9 1.0

Magnesium binding site 5 out of 8 in 2v69

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Magnesium binding site 5 out of 8 in the Crystal Structure of Chlamydomonas Reinhardtii Rubisco with A Large- Subunit Mutation D473E


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 Chlamydomonas Reinhardtii Rubisco with A Large- Subunit Mutation D473E within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Mg1470

b:46.9
occ:1.00
OE1 E:GLU204 2.0 49.0 1.0
OQ1 E:KCX201 2.0 52.7 1.0
OD1 E:ASP203 2.0 50.1 1.0
O7 E:CAP1471 2.1 57.1 1.0
O3 E:CAP1471 2.2 53.9 1.0
O2 E:CAP1471 2.3 55.9 1.0
C E:CAP1471 2.9 56.4 1.0
C2 E:CAP1471 2.9 55.9 1.0
CD E:GLU204 3.1 49.1 1.0
C3 E:CAP1471 3.1 55.3 1.0
CX E:KCX201 3.1 51.8 1.0
CG E:ASP203 3.2 48.8 1.0
NZ E:LYS177 3.6 46.4 1.0
OQ2 E:KCX201 3.6 53.0 1.0
OE2 E:GLU204 3.6 49.9 1.0
N E:GLU204 3.7 46.2 1.0
ND2 F:ASN123 3.8 50.7 1.0
OD2 E:ASP203 3.8 51.5 1.0
NE2 E:HIS294 4.0 45.1 1.0
O6 E:CAP1471 4.1 56.9 1.0
CG2 E:THR173 4.1 49.4 1.0
NZ E:LYS175 4.1 44.9 1.0
NZ E:KCX201 4.2 49.7 1.0
CA E:ASP203 4.2 46.8 1.0
CB E:ASP203 4.2 47.1 1.0
CG E:GLU204 4.3 47.5 1.0
C4 E:CAP1471 4.4 55.6 1.0
CB E:GLU204 4.4 45.9 1.0
C1 E:CAP1471 4.4 55.9 1.0
C E:ASP203 4.5 46.5 1.0
OG1 E:THR173 4.6 49.7 1.0
CD2 E:HIS294 4.7 44.0 1.0
CA E:GLU204 4.7 45.8 1.0
C5 E:CAP1471 4.8 55.2 1.0
CB E:THR173 4.9 49.2 1.0
O1 E:CAP1471 4.9 54.3 1.0
CE1 E:HIS294 4.9 43.9 1.0
CE E:LYS177 5.0 45.5 1.0

Magnesium binding site 6 out of 8 in 2v69

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Magnesium binding site 6 out of 8 in the Crystal Structure of Chlamydomonas Reinhardtii Rubisco with A Large- Subunit Mutation D473E


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 Chlamydomonas Reinhardtii Rubisco with A Large- Subunit Mutation D473E within 5.0Å range:
probe atom residue distance (Å) B Occ
F:Mg1470

b:47.4
occ:1.00
OD1 F:ASP203 2.0 50.7 1.0
OE1 F:GLU204 2.0 49.3 1.0
OQ1 F:KCX201 2.0 53.3 1.0
O2 F:CAP1471 2.1 55.6 1.0
O3 F:CAP1471 2.2 53.5 1.0
O7 F:CAP1471 2.3 57.0 1.0
C2 F:CAP1471 2.9 55.9 1.0
C F:CAP1471 3.0 56.3 1.0
CG F:ASP203 3.0 49.1 1.0
C3 F:CAP1471 3.1 55.3 1.0
CD F:GLU204 3.1 49.8 1.0
CX F:KCX201 3.2 51.6 1.0
NZ F:LYS177 3.6 46.4 1.0
OE2 F:GLU204 3.6 50.7 1.0
OQ2 F:KCX201 3.6 52.8 1.0
OD2 F:ASP203 3.7 51.1 1.0
N F:GLU204 3.7 46.3 1.0
ND2 E:ASN123 3.9 51.0 1.0
CG2 F:THR173 3.9 49.3 1.0
NE2 F:HIS294 4.0 45.1 1.0
NZ F:LYS175 4.0 45.2 1.0
CA F:ASP203 4.1 46.7 1.0
CB F:ASP203 4.1 47.3 1.0
NZ F:KCX201 4.2 49.2 1.0
O6 F:CAP1471 4.2 56.5 1.0
C1 F:CAP1471 4.3 56.0 1.0
CG F:GLU204 4.3 47.6 1.0
C4 F:CAP1471 4.4 55.4 1.0
C F:ASP203 4.4 46.4 1.0
OG1 F:THR173 4.5 49.0 1.0
CB F:GLU204 4.5 46.2 1.0
CD2 F:HIS294 4.6 44.3 1.0
CA F:GLU204 4.7 46.0 1.0
CB F:THR173 4.8 49.0 1.0
C5 F:CAP1471 4.8 54.9 1.0
O1 F:CAP1471 4.8 54.3 1.0
CE1 F:HIS294 4.9 44.4 1.0
CE F:LYS177 5.0 45.9 1.0

Magnesium binding site 7 out of 8 in 2v69

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Magnesium binding site 7 out of 8 in the Crystal Structure of Chlamydomonas Reinhardtii Rubisco with A Large- Subunit Mutation D473E


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 Chlamydomonas Reinhardtii Rubisco with A Large- Subunit Mutation D473E within 5.0Å range:
probe atom residue distance (Å) B Occ
G:Mg1470

b:46.1
occ:1.00
OQ1 G:KCX201 1.8 52.7 1.0
OE1 G:GLU204 1.9 49.9 1.0
OD1 G:ASP203 2.0 50.2 1.0
O3 G:CAP1471 2.0 53.4 1.0
O2 G:CAP1471 2.3 56.5 1.0
O7 G:CAP1471 2.3 56.9 1.0
C2 G:CAP1471 2.9 56.1 1.0
C3 G:CAP1471 3.0 55.5 1.0
CX G:KCX201 3.0 52.1 1.0
C G:CAP1471 3.0 56.3 1.0
CD G:GLU204 3.1 50.0 1.0
CG G:ASP203 3.2 49.2 1.0
OQ2 G:KCX201 3.5 53.3 1.0
NZ G:LYS177 3.6 46.1 1.0
OE2 G:GLU204 3.7 50.6 1.0
N G:GLU204 3.7 46.2 1.0
NE2 G:HIS294 3.8 45.3 1.0
ND2 H:ASN123 3.9 51.1 1.0
OD2 G:ASP203 3.9 51.5 1.0
CG2 G:THR173 4.0 49.4 1.0
NZ G:KCX201 4.1 49.9 1.0
CA G:ASP203 4.1 46.9 1.0
NZ G:LYS175 4.2 45.1 1.0
O6 G:CAP1471 4.2 56.3 1.0
CB G:ASP203 4.2 47.2 1.0
CG G:GLU204 4.3 47.4 1.0
C4 G:CAP1471 4.3 55.1 1.0
CB G:GLU204 4.3 46.0 1.0
C1 G:CAP1471 4.4 55.9 1.0
CD2 G:HIS294 4.4 43.5 1.0
C G:ASP203 4.4 46.4 1.0
OG1 G:THR173 4.5 49.2 1.0
CA G:GLU204 4.6 45.9 1.0
C5 G:CAP1471 4.7 54.5 1.0
CE1 G:HIS294 4.7 44.1 1.0
CB G:THR173 4.8 49.3 1.0
O1 G:CAP1471 4.9 54.2 1.0

Magnesium binding site 8 out of 8 in 2v69

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Magnesium binding site 8 out of 8 in the Crystal Structure of Chlamydomonas Reinhardtii Rubisco with A Large- Subunit Mutation D473E


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 Chlamydomonas Reinhardtii Rubisco with A Large- Subunit Mutation D473E within 5.0Å range:
probe atom residue distance (Å) B Occ
H:Mg1470

b:47.0
occ:1.00
OQ1 H:KCX201 1.9 53.1 1.0
OD1 H:ASP203 1.9 50.3 1.0
OE1 H:GLU204 2.1 50.2 1.0
O3 H:CAP1471 2.2 54.0 1.0
O7 H:CAP1471 2.3 56.8 1.0
O2 H:CAP1471 2.3 55.6 1.0
C2 H:CAP1471 2.9 56.0 1.0
C H:CAP1471 3.0 56.2 1.0
CX H:KCX201 3.0 52.4 1.0
CG H:ASP203 3.0 48.7 1.0
C3 H:CAP1471 3.1 55.6 1.0
CD H:GLU204 3.1 50.0 1.0
OQ2 H:KCX201 3.5 53.3 1.0
NZ H:LYS177 3.5 46.1 1.0
OE2 H:GLU204 3.7 50.7 1.0
N H:GLU204 3.7 46.1 1.0
OD2 H:ASP203 3.7 51.3 1.0
NE2 H:HIS294 3.9 45.4 1.0
CG2 H:THR173 4.0 49.5 1.0
ND2 G:ASN123 4.0 50.6 1.0
NZ H:LYS175 4.0 44.9 1.0
CA H:ASP203 4.0 46.5 1.0
CB H:ASP203 4.1 46.9 1.0
NZ H:KCX201 4.1 50.3 1.0
O6 H:CAP1471 4.2 56.6 1.0
CG H:GLU204 4.3 47.5 1.0
C4 H:CAP1471 4.4 55.1 1.0
CB H:GLU204 4.4 46.1 1.0
C1 H:CAP1471 4.4 56.2 1.0
OG1 H:THR173 4.4 49.6 1.0
C H:ASP203 4.4 46.2 1.0
CD2 H:HIS294 4.5 44.2 1.0
CA H:GLU204 4.7 45.9 1.0
CB H:THR173 4.7 49.1 1.0
C5 H:CAP1471 4.8 54.3 1.0
O1 H:CAP1471 4.9 54.5 1.0
CE1 H:HIS294 4.9 44.0 1.0
CE H:LYS177 5.0 46.2 1.0

Reference:

S.Karkehabadi, S.Satagopan, T.C.Taylor, R.J.Spreitzer, I.Andersson. Structural Analysis of Altered Large-Subunit Loop-6-Carboxy-Terminus Interactions That Influence Catalytic Efficiency and CO2-O2 Specificity of Ribulose-1,5-Bisphosphate Carboxylase Oxygenase Biochemistry V. 46 11080 2007.
ISSN: ISSN 0006-2960
PubMed: 17824672
DOI: 10.1021/BI701063F
Page generated: Wed Aug 14 05:00:02 2024

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