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Magnesium in PDB 2vdi: Crystal Structure of Chlamydomonas Reinhardtii Rubisco with A Large- Subunit C192S Mutation

Enzymatic activity of Crystal Structure of Chlamydomonas Reinhardtii Rubisco with A Large- Subunit C192S Mutation

All present enzymatic activity of Crystal Structure of Chlamydomonas Reinhardtii Rubisco with A Large- Subunit C192S Mutation:
4.1.1.39;

Protein crystallography data

The structure of Crystal Structure of Chlamydomonas Reinhardtii Rubisco with A Large- Subunit C192S Mutation, PDB code: 2vdi was solved by M.-J.Garcia-Murria, S.Karkehabadi, J.Marin-Navarro, S.Satagopan, I.Andersson, R.J.Spreitzer, J.Moreno, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 2.65
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 120.831, 178.206, 122.917, 90.00, 117.76, 90.00
R / Rfree (%) 20.5 / 23.4

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of Chlamydomonas Reinhardtii Rubisco with A Large- Subunit C192S Mutation (pdb code 2vdi). 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 C192S Mutation, PDB code: 2vdi:
Jump to Magnesium binding site number: 1; 2; 3; 4; 5; 6; 7; 8;

Magnesium binding site 1 out of 8 in 2vdi

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Magnesium binding site 1 out of 8 in the Crystal Structure of Chlamydomonas Reinhardtii Rubisco with A Large- Subunit C192S Mutation


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 C192S Mutation within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1476

b:8.5
occ:1.00
OD1 A:ASP203 1.9 10.7 1.0
OE1 A:GLU204 2.0 11.5 1.0
OQ1 A:KCX201 2.1 9.2 1.0
O2 A:CAP1477 2.2 12.4 1.0
O7 A:CAP1477 2.2 12.7 1.0
O3 A:CAP1477 2.2 13.2 1.0
C2 A:CAP1477 2.9 12.8 1.0
C A:CAP1477 2.9 12.8 1.0
CG A:ASP203 3.1 10.7 1.0
C3 A:CAP1477 3.1 13.2 1.0
CX A:KCX201 3.1 9.4 1.0
CD A:GLU204 3.1 11.5 1.0
OQ2 A:KCX201 3.4 10.8 1.0
NZ A:LYS177 3.6 8.0 1.0
OE2 A:GLU204 3.6 12.9 1.0
N A:GLU204 3.7 9.3 1.0
OD2 A:ASP203 3.7 12.5 1.0
NZ A:LYS175 3.9 9.5 1.0
CG2 A:THR173 3.9 11.4 1.0
ND2 B:ASN123 4.0 14.7 1.0
NE2 A:HIS294 4.0 6.3 1.0
CA A:ASP203 4.1 9.7 1.0
CB A:ASP203 4.1 10.0 1.0
O6 A:CAP1477 4.2 12.9 1.0
NZ A:KCX201 4.3 8.8 1.0
C1 A:CAP1477 4.3 12.1 1.0
C4 A:CAP1477 4.3 13.2 1.0
CG A:GLU204 4.3 10.0 1.0
C A:ASP203 4.4 9.6 1.0
CB A:GLU204 4.5 9.1 1.0
OG1 A:THR173 4.5 11.9 1.0
CB A:THR173 4.7 11.7 1.0
CD2 A:HIS294 4.7 6.5 1.0
CA A:GLU204 4.7 9.1 1.0
O1 A:CAP1477 4.8 10.8 1.0
C5 A:CAP1477 4.8 13.1 1.0
CE1 A:HIS294 5.0 6.3 1.0

Magnesium binding site 2 out of 8 in 2vdi

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Magnesium binding site 2 out of 8 in the Crystal Structure of Chlamydomonas Reinhardtii Rubisco with A Large- Subunit C192S Mutation


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 C192S Mutation within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg1476

b:8.6
occ:1.00
OD1 B:ASP203 2.0 10.8 1.0
OE1 B:GLU204 2.0 11.9 1.0
OQ1 B:KCX201 2.1 9.3 1.0
O7 B:CAP1477 2.2 12.5 1.0
O3 B:CAP1477 2.2 13.2 1.0
O2 B:CAP1477 2.3 12.4 1.0
C2 B:CAP1477 2.9 12.9 1.0
C B:CAP1477 2.9 12.9 1.0
C3 B:CAP1477 3.1 13.4 1.0
CX B:KCX201 3.1 9.4 1.0
CG B:ASP203 3.1 10.6 1.0
CD B:GLU204 3.2 11.7 1.0
OQ2 B:KCX201 3.3 11.0 1.0
NZ B:LYS177 3.6 8.1 1.0
OE2 B:GLU204 3.7 13.1 1.0
N B:GLU204 3.7 9.4 1.0
OD2 B:ASP203 3.8 12.2 1.0
NZ B:LYS175 3.8 9.6 1.0
CG2 B:THR173 3.9 11.4 1.0
ND2 A:ASN123 4.0 15.1 1.0
NE2 B:HIS294 4.1 6.2 1.0
CA B:ASP203 4.1 9.8 1.0
O6 B:CAP1477 4.1 13.2 1.0
CB B:ASP203 4.1 9.8 1.0
NZ B:KCX201 4.3 8.4 1.0
C4 B:CAP1477 4.3 13.1 1.0
C1 B:CAP1477 4.3 12.0 1.0
CG B:GLU204 4.4 10.2 1.0
C B:ASP203 4.4 9.6 1.0
OG1 B:THR173 4.5 12.2 1.0
CB B:GLU204 4.5 9.1 1.0
CB B:THR173 4.7 11.6 1.0
CD2 B:HIS294 4.7 6.8 1.0
CA B:GLU204 4.8 9.2 1.0
O1 B:CAP1477 4.8 11.0 1.0
C5 B:CAP1477 4.9 12.9 1.0
O A:HOH2038 5.0 8.8 1.0
CE B:LYS177 5.0 8.7 1.0

Magnesium binding site 3 out of 8 in 2vdi

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Magnesium binding site 3 out of 8 in the Crystal Structure of Chlamydomonas Reinhardtii Rubisco with A Large- Subunit C192S Mutation


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 C192S Mutation within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mg1476

b:9.2
occ:1.00
OD1 C:ASP203 1.9 10.5 1.0
OE1 C:GLU204 2.0 10.9 1.0
OQ1 C:KCX201 2.1 9.3 1.0
O7 C:CAP1477 2.2 12.7 1.0
O3 C:CAP1477 2.2 13.3 1.0
O2 C:CAP1477 2.3 12.5 1.0
C2 C:CAP1477 2.9 12.9 1.0
C C:CAP1477 2.9 13.0 1.0
CG C:ASP203 3.0 10.5 1.0
CD C:GLU204 3.1 11.4 1.0
C3 C:CAP1477 3.1 13.2 1.0
CX C:KCX201 3.2 9.3 1.0
OQ2 C:KCX201 3.4 10.9 1.0
OE2 C:GLU204 3.6 13.1 1.0
NZ C:LYS177 3.6 7.5 1.0
N C:GLU204 3.7 9.3 1.0
OD2 C:ASP203 3.8 12.1 1.0
NZ C:LYS175 3.9 9.8 1.0
ND2 D:ASN123 3.9 15.3 1.0
NE2 C:HIS294 4.0 6.1 1.0
CG2 C:THR173 4.0 11.5 1.0
CA C:ASP203 4.0 9.7 1.0
CB C:ASP203 4.1 10.1 1.0
O6 C:CAP1477 4.2 13.1 1.0
CG C:GLU204 4.3 9.8 1.0
NZ C:KCX201 4.3 8.9 1.0
C4 C:CAP1477 4.3 13.5 1.0
C1 C:CAP1477 4.4 12.1 1.0
C C:ASP203 4.4 9.6 1.0
CB C:GLU204 4.4 9.1 1.0
OG1 C:THR173 4.5 11.8 1.0
CD2 C:HIS294 4.6 6.6 1.0
CA C:GLU204 4.7 9.0 1.0
CB C:THR173 4.8 11.7 1.0
C5 C:CAP1477 4.8 13.2 1.0
CE1 C:HIS294 4.9 6.4 1.0
O1 C:CAP1477 4.9 11.0 1.0
CE C:LYS177 5.0 8.0 1.0

Magnesium binding site 4 out of 8 in 2vdi

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Magnesium binding site 4 out of 8 in the Crystal Structure of Chlamydomonas Reinhardtii Rubisco with A Large- Subunit C192S Mutation


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 C192S Mutation within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Mg1476

b:8.1
occ:1.00
OD1 D:ASP203 1.9 10.9 1.0
OE1 D:GLU204 2.1 11.9 1.0
OQ1 D:KCX201 2.1 8.9 1.0
O7 D:CAP1477 2.2 13.1 1.0
O3 D:CAP1477 2.2 13.4 1.0
O2 D:CAP1477 2.3 12.5 1.0
C D:CAP1477 2.9 13.0 1.0
C2 D:CAP1477 2.9 12.8 1.0
CG D:ASP203 3.0 10.9 1.0
CX D:KCX201 3.1 9.5 1.0
C3 D:CAP1477 3.1 13.4 1.0
CD D:GLU204 3.2 11.7 1.0
OQ2 D:KCX201 3.4 11.0 1.0
NZ D:LYS177 3.6 8.0 1.0
OE2 D:GLU204 3.7 13.5 1.0
N D:GLU204 3.7 9.3 1.0
OD2 D:ASP203 3.7 12.7 1.0
NZ D:LYS175 3.9 9.4 1.0
CG2 D:THR173 3.9 11.3 1.0
ND2 C:ASN123 4.0 15.1 1.0
NE2 D:HIS294 4.1 6.3 1.0
CA D:ASP203 4.1 9.7 1.0
O6 D:CAP1477 4.1 13.0 1.0
CB D:ASP203 4.1 9.9 1.0
NZ D:KCX201 4.2 9.1 1.0
CG D:GLU204 4.3 9.9 1.0
C1 D:CAP1477 4.3 12.2 1.0
C4 D:CAP1477 4.4 13.1 1.0
OG1 D:THR173 4.4 11.8 1.0
CB D:GLU204 4.4 9.2 1.0
C D:ASP203 4.4 9.6 1.0
CB D:THR173 4.6 11.6 1.0
CD2 D:HIS294 4.7 6.7 1.0
CA D:GLU204 4.7 9.1 1.0
O1 D:CAP1477 4.8 10.6 1.0
C5 D:CAP1477 4.9 12.9 1.0

Magnesium binding site 5 out of 8 in 2vdi

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Magnesium binding site 5 out of 8 in the Crystal Structure of Chlamydomonas Reinhardtii Rubisco with A Large- Subunit C192S Mutation


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 C192S Mutation within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Mg1476

b:8.7
occ:1.00
OD1 E:ASP203 1.9 10.7 1.0
OQ1 E:KCX201 2.1 8.9 1.0
OE1 E:GLU204 2.1 11.3 1.0
O2 E:CAP1477 2.2 12.2 1.0
O3 E:CAP1477 2.3 13.0 1.0
O7 E:CAP1477 2.3 12.7 1.0
C2 E:CAP1477 2.9 12.7 1.0
C E:CAP1477 3.0 12.8 1.0
CG E:ASP203 3.0 10.6 1.0
CX E:KCX201 3.1 9.4 1.0
C3 E:CAP1477 3.1 13.2 1.0
CD E:GLU204 3.2 11.4 1.0
OQ2 E:KCX201 3.4 10.8 1.0
OD2 E:ASP203 3.6 12.4 1.0
NZ E:LYS177 3.7 8.1 1.0
OE2 E:GLU204 3.7 13.1 1.0
N E:GLU204 3.7 9.3 1.0
NZ E:LYS175 3.9 9.2 1.0
CG2 E:THR173 3.9 11.1 1.0
CA E:ASP203 4.0 9.7 1.0
ND2 F:ASN123 4.1 14.9 1.0
CB E:ASP203 4.1 9.9 1.0
NE2 E:HIS294 4.1 6.5 1.0
O6 E:CAP1477 4.2 13.0 1.0
NZ E:KCX201 4.2 8.7 1.0
C1 E:CAP1477 4.3 12.0 1.0
C4 E:CAP1477 4.4 13.2 1.0
CG E:GLU204 4.4 9.8 1.0
OG1 E:THR173 4.4 12.0 1.0
C E:ASP203 4.4 9.6 1.0
CB E:GLU204 4.5 9.0 1.0
CB E:THR173 4.7 11.6 1.0
CD2 E:HIS294 4.7 6.4 1.0
CA E:GLU204 4.7 9.0 1.0
O1 E:CAP1477 4.8 10.8 1.0
C5 E:CAP1477 4.8 13.1 1.0
CE1 E:HIS294 5.0 6.3 1.0

Magnesium binding site 6 out of 8 in 2vdi

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Magnesium binding site 6 out of 8 in the Crystal Structure of Chlamydomonas Reinhardtii Rubisco with A Large- Subunit C192S Mutation


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 C192S Mutation within 5.0Å range:
probe atom residue distance (Å) B Occ
F:Mg1476

b:8.8
occ:1.00
OD1 F:ASP203 1.8 10.7 1.0
OE1 F:GLU204 2.0 11.7 1.0
OQ1 F:KCX201 2.1 9.2 1.0
O7 F:CAP1477 2.3 12.4 1.0
O3 F:CAP1477 2.3 13.5 1.0
O2 F:CAP1477 2.3 12.6 1.0
C2 F:CAP1477 3.0 12.8 1.0
CG F:ASP203 3.0 10.7 1.0
C F:CAP1477 3.0 12.8 1.0
CD F:GLU204 3.1 11.6 1.0
CX F:KCX201 3.1 9.3 1.0
C3 F:CAP1477 3.2 13.1 1.0
OQ2 F:KCX201 3.4 10.8 1.0
OE2 F:GLU204 3.6 12.8 1.0
NZ F:LYS177 3.6 8.2 1.0
N F:GLU204 3.6 9.3 1.0
OD2 F:ASP203 3.7 12.6 1.0
CG2 F:THR173 3.9 11.8 1.0
NZ F:LYS175 3.9 9.8 1.0
CA F:ASP203 4.0 9.8 1.0
ND2 E:ASN123 4.0 15.3 1.0
CB F:ASP203 4.0 10.0 1.0
NE2 F:HIS294 4.1 6.6 1.0
O6 F:CAP1477 4.2 13.0 1.0
NZ F:KCX201 4.2 8.6 1.0
CG F:GLU204 4.3 10.1 1.0
C F:ASP203 4.3 9.7 1.0
CB F:GLU204 4.4 9.1 1.0
C1 F:CAP1477 4.4 12.2 1.0
C4 F:CAP1477 4.4 13.3 1.0
OG1 F:THR173 4.5 11.8 1.0
CA F:GLU204 4.6 9.2 1.0
CB F:THR173 4.7 11.6 1.0
CD2 F:HIS294 4.8 6.3 1.0
O1 F:CAP1477 4.9 11.2 1.0
C5 F:CAP1477 4.9 13.2 1.0
CE F:LYS177 5.0 8.6 1.0

Magnesium binding site 7 out of 8 in 2vdi

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Magnesium binding site 7 out of 8 in the Crystal Structure of Chlamydomonas Reinhardtii Rubisco with A Large- Subunit C192S Mutation


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 C192S Mutation within 5.0Å range:
probe atom residue distance (Å) B Occ
G:Mg1476

b:9.0
occ:1.00
OD1 G:ASP203 1.9 10.8 1.0
OE1 G:GLU204 1.9 11.3 1.0
OQ1 G:KCX201 2.1 9.3 1.0
O3 G:CAP1477 2.2 12.9 1.0
O2 G:CAP1477 2.3 12.8 1.0
O7 G:CAP1477 2.3 12.6 1.0
C2 G:CAP1477 2.9 12.8 1.0
C G:CAP1477 3.0 12.7 1.0
CD G:GLU204 3.0 11.1 1.0
CG G:ASP203 3.1 10.9 1.0
C3 G:CAP1477 3.1 13.2 1.0
CX G:KCX201 3.1 9.4 1.0
OQ2 G:KCX201 3.4 11.0 1.0
OE2 G:GLU204 3.6 12.7 1.0
NZ G:LYS177 3.6 8.2 1.0
N G:GLU204 3.6 9.4 1.0
OD2 G:ASP203 3.8 12.6 1.0
NZ G:LYS175 3.9 9.1 1.0
ND2 H:ASN123 3.9 15.0 1.0
CG2 G:THR173 4.0 11.5 1.0
CA G:ASP203 4.0 9.8 1.0
NE2 G:HIS294 4.0 5.9 1.0
CB G:ASP203 4.1 9.9 1.0
O6 G:CAP1477 4.2 12.8 1.0
CG G:GLU204 4.3 9.8 1.0
NZ G:KCX201 4.3 8.8 1.0
C G:ASP203 4.4 9.7 1.0
C4 G:CAP1477 4.4 13.2 1.0
C1 G:CAP1477 4.4 11.8 1.0
CB G:GLU204 4.4 8.9 1.0
OG1 G:THR173 4.5 12.0 1.0
CA G:GLU204 4.7 9.2 1.0
CD2 G:HIS294 4.7 6.6 1.0
CB G:THR173 4.7 11.7 1.0
C5 G:CAP1477 4.9 12.9 1.0
O1 G:CAP1477 4.9 10.5 1.0
CE1 G:HIS294 4.9 6.1 1.0
CE G:LYS177 4.9 8.6 1.0

Magnesium binding site 8 out of 8 in 2vdi

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Magnesium binding site 8 out of 8 in the Crystal Structure of Chlamydomonas Reinhardtii Rubisco with A Large- Subunit C192S Mutation


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 C192S Mutation within 5.0Å range:
probe atom residue distance (Å) B Occ
H:Mg1476

b:8.0
occ:1.00
OD1 H:ASP203 1.9 10.4 1.0
OE1 H:GLU204 2.0 11.6 1.0
OQ1 H:KCX201 2.2 9.1 1.0
O2 H:CAP1477 2.3 12.2 1.0
O3 H:CAP1477 2.3 13.0 1.0
O7 H:CAP1477 2.3 12.5 1.0
C2 H:CAP1477 2.9 12.7 1.0
C H:CAP1477 3.0 12.7 1.0
CG H:ASP203 3.0 10.5 1.0
CD H:GLU204 3.0 11.3 1.0
C3 H:CAP1477 3.1 13.2 1.0
CX H:KCX201 3.2 9.2 1.0
OQ2 H:KCX201 3.5 11.0 1.0
OE2 H:GLU204 3.6 12.2 1.0
NZ H:LYS177 3.6 8.1 1.0
N H:GLU204 3.7 9.3 1.0
OD2 H:ASP203 3.7 12.7 1.0
ND2 G:ASN123 3.9 14.8 1.0
NZ H:LYS175 4.0 9.0 1.0
CG2 H:THR173 4.0 11.6 1.0
NE2 H:HIS294 4.0 6.1 1.0
CA H:ASP203 4.1 9.8 1.0
CB H:ASP203 4.1 10.1 1.0
O6 H:CAP1477 4.2 12.6 1.0
CG H:GLU204 4.3 9.9 1.0
C4 H:CAP1477 4.3 13.2 1.0
C1 H:CAP1477 4.4 12.0 1.0
NZ H:KCX201 4.4 8.6 1.0
CB H:GLU204 4.4 9.1 1.0
C H:ASP203 4.4 9.6 1.0
OG1 H:THR173 4.6 11.8 1.0
CA H:GLU204 4.7 9.1 1.0
CD2 H:HIS294 4.7 6.5 1.0
CB H:THR173 4.8 11.8 1.0
C5 H:CAP1477 4.8 13.0 1.0
O1 H:CAP1477 4.9 10.4 1.0
CE1 H:HIS294 4.9 6.4 1.0
CE H:LYS177 5.0 7.8 1.0

Reference:

M.-J.Garcia-Murria, S.Karkehabadi, J.Marin-Navarro, S.Satagopan, I.Andersson, R.J.Spreitzer, J.Moreno. Structural and Functional Consequences of the Replacement of Proximal Residues Cys-172 and Cys-192 in the Large Subunit of Ribulose 1,5-Bisphosphate Carboxylase/Oxygenase From Chlamydomonas Reinhardtii Biochem.J. V. 411 241 2008.
ISSN: ISSN 0264-6021
PubMed: 18072944
DOI: 10.1042/BJ20071422
Page generated: Wed Aug 14 05:08:46 2024

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