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Manganese in PDB 9cq5: Mn-Bound Rubisco From Spinach with Cabp Inhibitor

Enzymatic activity of Mn-Bound Rubisco From Spinach with Cabp Inhibitor

All present enzymatic activity of Mn-Bound Rubisco From Spinach with Cabp Inhibitor:
4.1.1.39;

Protein crystallography data

The structure of Mn-Bound Rubisco From Spinach with Cabp Inhibitor, PDB code: 9cq5 was solved by R.W.Voland, K.M.Lancaster, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 99.51 / 2.50
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 218.029, 218.893, 111.84, 90, 90, 90
R / Rfree (%) 19.7 / 24.2

Manganese Binding Sites:

The binding sites of Manganese atom in the Mn-Bound Rubisco From Spinach with Cabp Inhibitor (pdb code 9cq5). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 8 binding sites of Manganese where determined in the Mn-Bound Rubisco From Spinach with Cabp Inhibitor, PDB code: 9cq5:
Jump to Manganese binding site number: 1; 2; 3; 4; 5; 6; 7; 8;

Manganese binding site 1 out of 8 in 9cq5

Go back to Manganese Binding Sites List in 9cq5
Manganese binding site 1 out of 8 in the Mn-Bound Rubisco From Spinach with Cabp Inhibitor


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Mn-Bound Rubisco From Spinach with Cabp Inhibitor within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn501

b:49.0
occ:1.00
O6 A:CAP502 1.8 49.2 1.0
OQ2 A:KCX201 1.9 47.0 1.0
OD1 A:ASP203 2.0 57.6 1.0
OE1 A:GLU204 2.1 43.7 1.0
O2 A:CAP502 2.4 51.7 1.0
O3 A:CAP502 2.5 42.5 1.0
C A:CAP502 2.7 50.6 1.0
CX A:KCX201 2.9 44.3 1.0
C2 A:CAP502 2.9 51.2 1.0
CD A:GLU204 3.1 48.5 1.0
OQ1 A:KCX201 3.2 41.4 1.0
CG A:ASP203 3.2 51.0 1.0
C3 A:CAP502 3.3 42.6 1.0
OE2 A:GLU204 3.5 50.8 1.0
OD2 A:ASP203 3.8 47.6 1.0
CG2 A:THR173 3.8 43.1 1.0
O7 A:CAP502 3.8 53.7 1.0
NE2 A:HIS294 3.9 43.4 1.0
N A:GLU204 4.0 42.1 1.0
ND2 B:ASN123 4.0 45.0 1.0
NZ A:KCX201 4.0 46.2 1.0
NZ A:LYS177 4.0 44.6 1.0
CB A:ASP203 4.3 49.5 1.0
CA A:ASP203 4.3 43.4 1.0
NZ A:LYS175 4.3 49.7 1.0
C4 A:CAP502 4.4 42.9 1.0
C1 A:CAP502 4.4 50.6 1.0
CG A:GLU204 4.4 42.2 1.0
CB A:GLU204 4.6 44.3 1.0
CE1 A:HIS294 4.7 40.5 1.0
CD2 A:HIS294 4.7 39.5 1.0
C A:ASP203 4.7 44.1 1.0
O1 A:CAP502 4.7 47.8 1.0
CB A:THR173 4.8 41.3 1.0
OG1 A:THR173 4.9 53.5 1.0
C5 A:CAP502 4.9 48.0 1.0
CA A:GLU204 4.9 44.3 1.0

Manganese binding site 2 out of 8 in 9cq5

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Manganese binding site 2 out of 8 in the Mn-Bound Rubisco From Spinach with Cabp Inhibitor


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Mn-Bound Rubisco From Spinach with Cabp Inhibitor within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mn501

b:54.6
occ:1.00
OQ1 B:KCX201 1.8 51.1 1.0
O6 B:CAP502 2.0 59.8 1.0
OD1 B:ASP203 2.2 61.8 1.0
OE1 B:GLU204 2.2 55.3 1.0
O2 B:CAP502 2.5 54.6 1.0
O3 B:CAP502 2.8 52.4 1.0
CX B:KCX201 2.9 54.9 1.0
C B:CAP502 2.9 52.1 1.0
C2 B:CAP502 3.1 57.9 1.0
OQ2 B:KCX201 3.3 52.9 1.0
CG B:ASP203 3.3 58.4 1.0
CD B:GLU204 3.3 56.4 1.0
C3 B:CAP502 3.5 56.4 1.0
NZ B:LYS175 3.7 55.9 1.0
NZ B:LYS177 3.7 57.7 1.0
OD2 B:ASP203 3.8 64.5 1.0
ND2 A:ASN123 3.9 49.4 1.0
OE2 B:GLU204 3.9 54.7 1.0
NE2 B:HIS294 3.9 46.4 1.0
NZ B:KCX201 4.0 55.4 1.0
N B:GLU204 4.0 51.2 1.0
CG2 B:THR173 4.0 55.8 1.0
O7 B:CAP502 4.0 49.0 1.0
CE B:LYS177 4.2 62.4 1.0
CB B:ASP203 4.5 50.9 1.0
CA B:ASP203 4.5 52.2 1.0
CG B:GLU204 4.5 51.1 1.0
C4 B:CAP502 4.5 52.8 1.0
C1 B:CAP502 4.5 62.2 1.0
CD2 B:HIS294 4.6 48.0 1.0
CB B:GLU204 4.6 50.2 1.0
C B:ASP203 4.8 55.7 1.0
CE1 B:HIS294 4.8 40.6 1.0
C5 B:CAP502 4.9 51.4 1.0
O1 B:CAP502 4.9 55.9 1.0
CA B:GLU204 4.9 49.5 1.0

Manganese binding site 3 out of 8 in 9cq5

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Manganese binding site 3 out of 8 in the Mn-Bound Rubisco From Spinach with Cabp Inhibitor


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 3 of Mn-Bound Rubisco From Spinach with Cabp Inhibitor within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mn501

b:46.2
occ:1.00
OD1 C:ASP203 2.0 44.2 1.0
OQ2 C:KCX201 2.0 38.1 1.0
OE1 C:GLU204 2.2 41.1 1.0
O6 C:CAP502 2.2 45.5 1.0
O3 C:CAP502 2.2 39.8 1.0
O2 C:CAP502 2.3 46.9 1.0
C C:CAP502 2.9 44.6 1.0
C2 C:CAP502 2.9 47.1 1.0
CX C:KCX201 3.0 39.6 1.0
CG C:ASP203 3.0 42.5 1.0
C3 C:CAP502 3.1 42.2 1.0
CD C:GLU204 3.4 39.3 1.0
OQ1 C:KCX201 3.4 46.9 1.0
OD2 C:ASP203 3.6 44.1 1.0
NZ C:LYS177 3.8 34.7 1.0
NZ C:LYS175 3.9 39.5 1.0
ND2 D:ASN123 3.9 38.0 1.0
OE2 C:GLU204 4.0 43.5 1.0
NE2 C:HIS294 4.0 41.7 1.0
N C:GLU204 4.0 35.9 1.0
O7 C:CAP502 4.0 41.9 1.0
CG2 C:THR173 4.1 36.2 1.0
NZ C:KCX201 4.1 43.7 1.0
CB C:ASP203 4.2 41.0 1.0
CA C:ASP203 4.3 37.7 1.0
C4 C:CAP502 4.3 42.0 1.0
C1 C:CAP502 4.4 41.8 1.0
CG C:GLU204 4.6 38.7 1.0
CB C:GLU204 4.6 35.8 1.0
CD2 C:HIS294 4.7 39.2 1.0
C C:ASP203 4.7 40.3 1.0
O1 C:CAP502 4.8 40.3 1.0
C5 C:CAP502 4.8 44.2 1.0
CE1 C:HIS294 4.9 39.4 1.0
CE C:LYS175 5.0 34.3 1.0
CA C:GLU204 5.0 36.5 1.0

Manganese binding site 4 out of 8 in 9cq5

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Manganese binding site 4 out of 8 in the Mn-Bound Rubisco From Spinach with Cabp Inhibitor


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 4 of Mn-Bound Rubisco From Spinach with Cabp Inhibitor within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Mn501

b:53.9
occ:1.00
OD1 D:ASP203 1.8 52.6 1.0
OQ2 D:KCX201 1.9 50.3 1.0
O2 D:CAP502 2.2 54.2 1.0
OE1 D:GLU204 2.2 45.8 1.0
O6 D:CAP502 2.4 55.6 1.0
O3 D:CAP502 2.6 46.7 1.0
C2 D:CAP502 3.0 51.9 1.0
CG D:ASP203 3.0 53.3 1.0
C D:CAP502 3.1 51.0 1.0
CX D:KCX201 3.1 48.1 1.0
C3 D:CAP502 3.3 52.7 1.0
CD D:GLU204 3.3 49.8 1.0
OQ1 D:KCX201 3.6 48.2 1.0
OD2 D:ASP203 3.8 51.6 1.0
OE2 D:GLU204 3.8 51.9 1.0
N D:GLU204 3.9 45.7 1.0
ND2 C:ASN123 4.0 45.5 1.0
CG2 D:THR173 4.0 50.3 1.0
NE2 D:HIS294 4.0 49.8 1.0
CE D:LYS177 4.0 50.2 1.0
CB D:ASP203 4.1 50.3 1.0
NZ D:LYS177 4.1 54.3 1.0
NZ D:LYS175 4.1 46.7 1.0
NZ D:KCX201 4.1 48.7 1.0
CA D:ASP203 4.2 50.3 1.0
O7 D:CAP502 4.3 55.2 1.0
C1 D:CAP502 4.4 52.7 1.0
CG D:GLU204 4.5 47.3 1.0
C4 D:CAP502 4.6 51.3 1.0
C D:ASP203 4.6 47.9 1.0
CB D:GLU204 4.6 44.9 1.0
CE1 D:HIS294 4.8 47.6 1.0
CD2 D:HIS294 4.8 43.0 1.0
O1 D:CAP502 4.8 52.5 1.0
CA D:GLU204 4.9 45.3 1.0

Manganese binding site 5 out of 8 in 9cq5

Go back to Manganese Binding Sites List in 9cq5
Manganese binding site 5 out of 8 in the Mn-Bound Rubisco From Spinach with Cabp Inhibitor


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 5 of Mn-Bound Rubisco From Spinach with Cabp Inhibitor within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Mn501

b:50.8
occ:1.00
OD1 E:ASP203 1.8 49.4 1.0
OE1 E:GLU204 2.0 34.7 1.0
O6 E:CAP502 2.0 45.9 1.0
OQ2 E:KCX201 2.0 45.3 1.0
O3 E:CAP502 2.6 37.5 1.0
O2 E:CAP502 2.6 44.9 1.0
C E:CAP502 2.8 39.8 1.0
CG E:ASP203 3.0 40.5 1.0
C2 E:CAP502 3.0 39.1 1.0
CD E:GLU204 3.1 41.6 1.0
CX E:KCX201 3.1 42.5 1.0
C3 E:CAP502 3.3 41.0 1.0
OQ1 E:KCX201 3.6 42.5 1.0
OE2 E:GLU204 3.7 44.2 1.0
OD2 E:ASP203 3.7 43.7 1.0
NE2 E:HIS294 3.8 31.1 1.0
NZ E:LYS177 3.8 42.7 1.0
N E:GLU204 3.9 43.1 1.0
ND2 F:ASN123 4.0 43.1 1.0
O7 E:CAP502 4.0 39.2 1.0
CB E:ASP203 4.1 38.3 1.0
NZ E:LYS175 4.1 34.0 1.0
CA E:ASP203 4.1 37.3 1.0
NZ E:KCX201 4.2 40.4 1.0
CG E:GLU204 4.3 38.5 1.0
CD2 E:HIS294 4.4 33.6 1.0
CG2 E:THR173 4.4 40.7 1.0
C1 E:CAP502 4.5 37.6 1.0
CB E:GLU204 4.5 32.6 1.0
C4 E:CAP502 4.5 41.1 1.0
C E:ASP203 4.6 44.6 1.0
O1 E:CAP502 4.8 33.7 1.0
CE1 E:HIS294 4.8 34.9 1.0
CA E:GLU204 4.9 42.3 1.0
OG1 E:THR173 4.9 43.2 1.0
C5 E:CAP502 4.9 39.9 1.0

Manganese binding site 6 out of 8 in 9cq5

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Manganese binding site 6 out of 8 in the Mn-Bound Rubisco From Spinach with Cabp Inhibitor


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 6 of Mn-Bound Rubisco From Spinach with Cabp Inhibitor within 5.0Å range:
probe atom residue distance (Å) B Occ
F:Mn501

b:50.0
occ:1.00
OE1 F:GLU204 1.8 57.7 1.0
O3 F:CAP502 2.2 51.0 1.0
OD1 F:ASP203 2.3 58.8 1.0
O2 F:CAP502 2.3 52.2 1.0
OQ2 F:KCX201 2.4 55.5 1.0
O6 F:CAP502 2.5 57.3 1.0
CD F:GLU204 2.8 57.9 1.0
C2 F:CAP502 2.9 54.7 1.0
OE2 F:GLU204 3.0 59.9 1.0
C F:CAP502 3.1 57.0 1.0
C3 F:CAP502 3.1 49.9 1.0
CG F:ASP203 3.3 57.1 1.0
CX F:KCX201 3.4 53.7 1.0
NZ F:LYS177 3.5 52.7 1.0
OQ1 F:KCX201 3.7 50.9 1.0
ND2 E:ASN123 3.8 46.3 1.0
NE2 F:HIS294 3.9 44.9 1.0
N F:GLU204 4.0 49.8 1.0
CB F:ASP203 4.1 53.0 1.0
CG F:GLU204 4.2 45.0 1.0
OD2 F:ASP203 4.2 53.4 1.0
NZ F:LYS175 4.2 50.3 1.0
C4 F:CAP502 4.3 51.2 1.0
CA F:ASP203 4.3 48.1 1.0
O7 F:CAP502 4.3 60.5 1.0
CG2 F:THR173 4.4 51.1 1.0
C1 F:CAP502 4.4 62.2 1.0
NZ F:KCX201 4.5 56.8 1.0
CD2 F:HIS294 4.6 44.2 1.0
CB F:GLU204 4.7 44.2 1.0
C F:ASP203 4.7 53.3 1.0
C5 F:CAP502 4.7 48.1 1.0
CE F:LYS177 4.8 55.1 1.0
O1 F:CAP502 4.9 56.8 1.0
CE1 F:HIS294 4.9 47.7 1.0
CA F:GLU204 5.0 45.7 1.0
CG E:ASN123 5.0 45.9 1.0

Manganese binding site 7 out of 8 in 9cq5

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Manganese binding site 7 out of 8 in the Mn-Bound Rubisco From Spinach with Cabp Inhibitor


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 7 of Mn-Bound Rubisco From Spinach with Cabp Inhibitor within 5.0Å range:
probe atom residue distance (Å) B Occ
G:Mn501

b:47.8
occ:1.00
OD1 G:ASP203 1.9 47.9 1.0
O2 G:CAP502 2.2 48.9 1.0
OE1 G:GLU204 2.2 37.4 1.0
O3 G:CAP502 2.3 44.3 1.0
O6 G:CAP502 2.4 48.4 1.0
OQ2 G:KCX201 2.6 44.9 1.0
C2 G:CAP502 2.9 45.3 1.0
C G:CAP502 3.0 44.2 1.0
CG G:ASP203 3.1 45.8 1.0
C3 G:CAP502 3.1 44.2 1.0
CD G:GLU204 3.3 37.6 1.0
CX G:KCX201 3.4 43.3 1.0
OQ1 G:KCX201 3.4 42.1 1.0
NZ G:LYS177 3.6 40.4 1.0
OD2 G:ASP203 3.7 39.2 1.0
OE2 G:GLU204 3.8 47.0 1.0
ND2 H:ASN123 3.9 37.4 1.0
CE1 G:HIS294 4.0 41.5 1.0
NZ G:LYS175 4.0 36.3 1.0
N G:GLU204 4.1 36.8 1.0
CG2 G:THR173 4.1 41.2 1.0
O7 G:CAP502 4.2 50.3 1.0
CB G:ASP203 4.3 40.8 1.0
C1 G:CAP502 4.3 44.1 1.0
CA G:ASP203 4.3 40.3 1.0
C4 G:CAP502 4.4 43.1 1.0
NZ G:KCX201 4.5 39.8 1.0
CG G:GLU204 4.5 37.4 1.0
ND1 G:HIS294 4.7 41.9 1.0
O1 G:CAP502 4.7 36.1 1.0
CB G:GLU204 4.7 35.5 1.0
C G:ASP203 4.8 44.2 1.0
C5 G:CAP502 4.8 45.9 1.0
CE G:LYS177 5.0 43.6 1.0
NE2 G:HIS294 5.0 37.9 1.0
OG1 G:THR173 5.0 45.5 1.0

Manganese binding site 8 out of 8 in 9cq5

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Manganese binding site 8 out of 8 in the Mn-Bound Rubisco From Spinach with Cabp Inhibitor


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 8 of Mn-Bound Rubisco From Spinach with Cabp Inhibitor within 5.0Å range:
probe atom residue distance (Å) B Occ
H:Mn501

b:63.6
occ:1.00
O3 H:CAP502 2.1 52.5 1.0
OQ2 H:KCX201 2.1 53.1 1.0
OD1 H:ASP203 2.2 47.3 1.0
OE1 H:GLU204 2.3 49.8 1.0
O2 H:CAP502 2.3 51.7 1.0
O6 H:CAP502 2.4 51.5 1.0
C2 H:CAP502 2.9 49.6 1.0
C H:CAP502 2.9 49.2 1.0
C3 H:CAP502 3.0 47.6 1.0
CX H:KCX201 3.2 52.0 1.0
CG H:ASP203 3.4 50.0 1.0
CD H:GLU204 3.4 49.1 1.0
NZ H:LYS177 3.6 47.2 1.0
OQ1 H:KCX201 3.6 54.3 1.0
ND2 G:ASN123 3.6 40.8 1.0
OD2 H:ASP203 4.0 54.5 1.0
NE2 H:HIS294 4.0 46.5 1.0
OE2 H:GLU204 4.0 47.7 1.0
C4 H:CAP502 4.1 47.8 1.0
O7 H:CAP502 4.1 51.8 1.0
N H:GLU204 4.1 45.8 1.0
NZ H:LYS175 4.2 53.4 1.0
NZ H:KCX201 4.3 45.8 1.0
C1 H:CAP502 4.4 48.5 1.0
CG2 H:THR173 4.4 42.0 1.0
CB H:ASP203 4.5 45.5 1.0
CA H:ASP203 4.5 43.2 1.0
C5 H:CAP502 4.6 45.2 1.0
CG H:GLU204 4.6 39.5 1.0
CB H:GLU204 4.7 39.6 1.0
CD2 H:HIS294 4.8 47.6 1.0
CE1 H:HIS294 4.8 44.7 1.0
O1 H:CAP502 4.8 50.6 1.0
CG G:ASN123 4.8 47.3 1.0
C H:ASP203 4.9 49.3 1.0
CE H:LYS177 5.0 46.2 1.0

Reference:

R.W.Voland, R.E.Coleman, K.M.Lancaster. The Structure of Mn(II)-Bound Rubisco From Spinacia Oleracea. J.Inorg.Biochem. V. 260 12682 2024.
ISSN: ISSN 0162-0134
PubMed: 39094246
DOI: 10.1016/J.JINORGBIO.2024.112682
Page generated: Sun Feb 9 08:28:48 2025

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