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Calcium 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:

Magnesium (Mg) 2 atoms
Cadmium (Cd) 4 atoms
Iron (Fe) 4 atoms
Copper (Cu) 6 atoms

Calcium Binding Sites:

The binding sites of Calcium 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 Calcium atom.
In total 2 binding sites of Calcium 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 Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in 3om3

Go back to Calcium Binding Sites List in 3om3
Calcium 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 Calcium with other atoms in the Ca 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:Ca553

b:34.8
occ:1.00
O A:ALA57 2.3 35.9 1.0
OE1 A:GLU54 2.3 37.2 1.0
O A:GLY59 2.3 36.2 1.0
O A:GLU54 2.3 36.3 1.0
OE1 A:GLN61 2.4 37.5 1.0
O A:HOH613 2.6 29.4 1.0
O A:HOH619 2.6 33.9 1.0
CD A:GLN61 3.4 36.5 1.0
C A:GLU54 3.4 36.1 1.0
C A:ALA57 3.4 36.6 1.0
CD A:GLU54 3.5 36.9 1.0
C A:GLY59 3.6 36.0 1.0
NE2 A:GLN61 3.8 36.3 1.0
CA A:GLU54 4.0 36.1 1.0
CG A:GLU54 4.1 35.8 1.0
N A:ALA57 4.1 38.3 1.0
CA A:VAL60 4.2 35.1 1.0
C A:PRO58 4.2 35.8 1.0
CA A:ALA57 4.3 37.2 1.0
N A:GLN61 4.3 35.6 1.0
O A:PRO58 4.3 35.8 1.0
N A:VAL60 4.4 35.5 1.0
N A:GLY59 4.4 36.0 1.0
N A:PRO58 4.4 36.3 1.0
OE2 A:GLU54 4.5 34.8 1.0
N A:LEU55 4.5 36.2 1.0
CA A:GLY59 4.6 35.8 1.0
CA A:PRO58 4.6 35.9 1.0
CB A:ALA57 4.7 36.9 1.0
O61 A:DMU1005 4.7 58.4 0.8
C A:VAL60 4.7 35.4 1.0
CB A:GLU54 4.7 36.0 1.0
CG A:GLN61 4.8 34.5 1.0
O A:MET53 4.8 36.8 1.0
CA A:LEU55 4.8 36.7 1.0
OD1 A:ASP485 4.9 33.5 1.0
CB A:GLN61 5.0 36.0 1.0
N A:MET56 5.0 38.4 1.0
C A:LEU55 5.0 37.7 1.0

Calcium binding site 2 out of 2 in 3om3

Go back to Calcium Binding Sites List in 3om3
Calcium 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 Calcium with other atoms in the Ca 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:Ca7

b:57.8
occ:1.00
O C:GLY59 2.3 58.1 1.0
O C:GLU54 2.3 56.5 1.0
O C:ALA57 2.3 56.6 1.0
OE1 C:GLU54 2.4 52.1 1.0
OE1 C:GLN61 2.4 59.8 1.0
O C:HOH573 2.6 60.1 1.0
O C:HOH565 2.6 48.5 1.0
C C:GLU54 3.4 56.4 1.0
CD C:GLN61 3.4 59.7 1.0
CD C:GLU54 3.4 54.5 1.0
C C:GLY59 3.5 57.9 1.0
C C:ALA57 3.6 57.2 1.0
NE2 C:GLN61 3.8 58.6 1.0
CG C:GLU54 3.8 55.5 1.0
CA C:GLU54 3.9 56.3 1.0
CA C:VAL60 4.0 58.9 1.0
N C:VAL60 4.2 58.3 1.0
N C:GLN61 4.2 60.5 1.0
C C:PRO58 4.3 57.2 1.0
N C:ALA57 4.3 57.6 1.0
O C:PRO58 4.4 57.2 1.0
N C:GLY59 4.4 57.3 1.0
CA C:ALA57 4.4 57.4 1.0
CB C:GLU54 4.5 56.1 1.0
N C:PRO58 4.5 57.2 1.0
N C:LEU55 4.5 56.5 1.0
OE2 C:GLU54 4.6 52.9 1.0
CA C:GLY59 4.6 57.6 1.0
OD1 C:ASP485 4.6 44.6 1.0
C C:VAL60 4.6 59.8 1.0
CA C:PRO58 4.6 57.2 1.0
CG C:GLN61 4.7 60.9 1.0
O C:MET53 4.8 57.3 1.0
CB C:ALA57 4.9 57.5 1.0
CA C:LEU55 4.9 56.6 1.0
O61 C:DMU10 4.9 54.3 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: Tue Jul 8 15:07:30 2025

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