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Magnesium in PDB 3om3: Catalytic Core Subunits (I and II) of Cytochrome C Oxidase From Rhodobacter Sphaeroides with K362M Mutation in the Reduced State

Enzymatic activity of Catalytic Core Subunits (I and II) of Cytochrome C Oxidase From Rhodobacter Sphaeroides with K362M Mutation in the Reduced State

All present enzymatic activity of Catalytic Core Subunits (I and II) of Cytochrome C Oxidase From Rhodobacter Sphaeroides with K362M Mutation in the Reduced State:
1.9.3.1;

Protein crystallography data

The structure of Catalytic Core Subunits (I and II) of Cytochrome C Oxidase From Rhodobacter Sphaeroides with K362M Mutation in the Reduced State, PDB code: 3om3 was solved by J.Liu, L.Qin, S.Ferguson-Miller, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 40.46 / 2.60
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 124.650, 132.365, 178.006, 90.00, 90.00, 90.00
R / Rfree (%) 19.8 / 22.9

Other elements in 3om3:

The structure of Catalytic Core Subunits (I and II) of Cytochrome C Oxidase From Rhodobacter Sphaeroides with K362M Mutation in the Reduced State also contains other interesting chemical elements:

Cadmium (Cd) 4 atoms
Iron (Fe) 4 atoms
Calcium (Ca) 2 atoms
Copper (Cu) 6 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Catalytic Core Subunits (I and II) of Cytochrome C Oxidase From Rhodobacter Sphaeroides with K362M Mutation in the Reduced State (pdb code 3om3). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Catalytic Core Subunits (I and II) of Cytochrome C Oxidase From Rhodobacter Sphaeroides with K362M Mutation in the Reduced State, PDB code: 3om3:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 3om3

Go back to Magnesium Binding Sites List in 3om3
Magnesium binding site 1 out of 2 in the Catalytic Core Subunits (I and II) of Cytochrome C Oxidase From Rhodobacter Sphaeroides with K362M Mutation in the Reduced State


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Catalytic Core Subunits (I and II) of Cytochrome C Oxidase From Rhodobacter Sphaeroides with K362M Mutation in the Reduced State within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg6

b:23.5
occ:1.00
OE1 B:GLU254 1.8 40.2 1.0
O B:HOH769 1.9 27.1 1.0
O B:HOH503 2.1 42.2 1.0
NE2 A:HIS411 2.2 34.5 1.0
O B:HOH766 2.2 45.9 1.0
OD2 A:ASP412 2.2 42.1 1.0
CD B:GLU254 3.0 40.9 1.0
CD2 A:HIS411 3.1 35.2 1.0
CE1 A:HIS411 3.1 34.8 1.0
CG A:ASP412 3.4 40.7 1.0
OE2 B:GLU254 3.6 40.8 1.0
O B:SER253 3.8 36.0 1.0
OD1 B:ASP229 4.0 43.8 1.0
CG B:GLU254 4.1 37.5 1.0
CB A:ASP412 4.1 37.9 1.0
OD2 B:ASP229 4.1 42.9 1.0
ND1 A:HIS411 4.2 34.4 1.0
CG A:HIS411 4.3 35.1 1.0
OD1 A:ASP412 4.3 43.4 1.0
CB B:GLU254 4.3 35.5 1.0
O A:HOH556 4.4 34.7 1.0
CG B:ASP229 4.5 42.8 1.0
OG1 A:THR337 4.5 47.7 1.0
O A:HOH557 4.7 45.8 1.0
CA B:GLU254 4.7 35.4 1.0
O A:HOH604 4.7 35.4 1.0
O A:HOH14 4.8 30.2 1.0
C B:SER253 4.9 35.8 1.0

Magnesium binding site 2 out of 2 in 3om3

Go back to Magnesium Binding Sites List in 3om3
Magnesium binding site 2 out of 2 in the Catalytic Core Subunits (I and II) of Cytochrome C Oxidase From Rhodobacter Sphaeroides with K362M Mutation in the Reduced State


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Catalytic Core Subunits (I and II) of Cytochrome C Oxidase From Rhodobacter Sphaeroides with K362M Mutation in the Reduced State within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mg6

b:31.0
occ:1.00
O C:HOH564 1.6 39.5 1.0
OD2 C:ASP412 2.0 47.1 1.0
OE1 D:GLU254 2.0 51.4 1.0
O C:HOH568 2.1 42.1 1.0
NE2 C:HIS411 2.3 42.3 1.0
O D:HOH304 2.3 41.7 1.0
CE1 C:HIS411 3.1 42.9 1.0
CG C:ASP412 3.2 45.6 1.0
CD D:GLU254 3.2 51.2 1.0
CD2 C:HIS411 3.3 44.0 1.0
O C:HOH584 3.8 39.6 1.0
O D:SER253 3.9 45.6 1.0
OD1 C:ASP412 4.0 45.9 1.0
OE2 D:GLU254 4.0 51.9 1.0
CB C:ASP412 4.2 43.7 1.0
ND1 C:HIS411 4.2 42.5 1.0
CG D:GLU254 4.3 47.7 1.0
OD1 D:ASP229 4.3 50.8 1.0
OD2 D:ASP229 4.3 50.1 1.0
CG C:HIS411 4.4 42.6 1.0
O D:HOH311 4.4 46.9 1.0
CB D:GLU254 4.5 46.0 1.0
O C:HOH571 4.6 45.3 1.0
O C:HOH580 4.7 42.2 1.0
CG D:ASP229 4.7 48.6 1.0
CA D:GLU254 4.8 46.0 1.0
OG1 C:THR337 4.8 52.7 1.0
CE2 C:TYR175 5.0 52.5 1.0

Reference:

J.Liu, L.Qin, S.Ferguson-Miller. Crystallographic and Online Spectral Evidence For Role of Conformational Change and Conserved Water in Cytochrome Oxidase Proton Pump. Proc.Natl.Acad.Sci.Usa V. 108 1284 2011.
ISSN: ISSN 0027-8424
PubMed: 21205904
DOI: 10.1073/PNAS.1012846108
Page generated: Thu Aug 15 08:26:21 2024

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