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Calcium in PDB 3omn: Catalytic Core Subunits (I and II) of Cytochrome C Oxidase From Rhodobacter Sphaeroides with D132A Mutation in the Reduced State

Enzymatic activity of Catalytic Core Subunits (I and II) of Cytochrome C Oxidase From Rhodobacter Sphaeroides with D132A Mutation in the Reduced State

All present enzymatic activity of Catalytic Core Subunits (I and II) of Cytochrome C Oxidase From Rhodobacter Sphaeroides with D132A 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 D132A Mutation in the Reduced State, PDB code: 3omn 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) 42.70 / 2.15
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 124.670, 132.033, 176.286, 90.00, 90.00, 90.00
R / Rfree (%) 19.8 / 21.9

Other elements in 3omn:

The structure of Catalytic Core Subunits (I and II) of Cytochrome C Oxidase From Rhodobacter Sphaeroides with D132A Mutation in the Reduced State also contains other interesting chemical elements:

Magnesium (Mg) 2 atoms
Cadmium (Cd) 4 atoms
Iron (Fe) 6 atoms
Chlorine (Cl) 2 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 D132A Mutation in the Reduced State (pdb code 3omn). 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 D132A Mutation in the Reduced State, PDB code: 3omn:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in 3omn

Go back to Calcium Binding Sites List in 3omn
Calcium binding site 1 out of 2 in the Catalytic Core Subunits (I and II) of Cytochrome C Oxidase From Rhodobacter Sphaeroides with D132A 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 D132A Mutation in the Reduced State within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca554

b:27.2
occ:1.00
O A:GLU54 2.3 25.8 1.0
O A:GLY59 2.3 26.2 1.0
O A:ALA57 2.3 28.3 1.0
OE1 A:GLU54 2.4 24.4 1.0
OE1 A:GLN61 2.4 30.7 1.0
O A:HOH810 2.6 22.8 1.0
O A:HOH803 2.6 23.8 1.0
C A:GLU54 3.4 25.6 1.0
CD A:GLU54 3.5 25.9 1.0
C A:ALA57 3.5 28.5 1.0
CD A:GLN61 3.5 30.7 1.0
C A:GLY59 3.6 26.9 1.0
CA A:GLU54 3.9 25.3 1.0
CG A:GLU54 4.0 24.8 1.0
NE2 A:GLN61 4.0 29.5 1.0
CA A:VAL60 4.2 26.7 1.0
N A:ALA57 4.2 29.2 1.0
N A:GLN61 4.2 28.6 1.0
N A:VAL60 4.3 26.4 1.0
C A:PRO58 4.3 27.8 1.0
CA A:ALA57 4.3 29.0 1.0
N A:GLY59 4.5 27.3 1.0
O A:PRO58 4.5 27.4 1.0
N A:LEU55 4.5 25.8 1.0
N A:PRO58 4.5 28.4 1.0
OE2 A:GLU54 4.6 25.3 1.0
CB A:GLU54 4.6 24.9 1.0
O61 A:DMU1005 4.6 44.5 0.8
C A:VAL60 4.6 27.9 1.0
CA A:GLY59 4.6 26.3 1.0
CA A:PRO58 4.7 27.9 1.0
O A:MET53 4.7 26.4 1.0
CB A:ALA57 4.8 28.5 1.0
CG A:GLN61 4.8 28.9 1.0
CA A:LEU55 4.8 26.2 1.0
OD1 A:ASP485 4.8 28.7 1.0
CB A:GLN61 4.9 29.6 1.0
C A:LEU55 5.0 27.1 1.0

Calcium binding site 2 out of 2 in 3omn

Go back to Calcium Binding Sites List in 3omn
Calcium binding site 2 out of 2 in the Catalytic Core Subunits (I and II) of Cytochrome C Oxidase From Rhodobacter Sphaeroides with D132A 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 D132A Mutation in the Reduced State within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Ca7

b:39.0
occ:1.00
OE1 C:GLU54 2.3 37.8 1.0
O C:GLU54 2.3 39.8 1.0
O C:ALA57 2.3 40.1 1.0
O C:GLY59 2.3 42.2 1.0
OE1 C:GLN61 2.4 45.2 1.0
O C:HOH568 2.5 33.8 1.0
O C:HOH580 2.6 41.4 1.0
C C:GLU54 3.4 39.7 1.0
CD C:GLU54 3.4 39.5 1.0
C C:ALA57 3.5 40.5 1.0
CD C:GLN61 3.5 45.6 1.0
C C:GLY59 3.5 42.2 1.0
NE2 C:GLN61 4.0 43.9 1.0
CA C:GLU54 4.0 39.8 1.0
CG C:GLU54 4.0 40.2 1.0
CA C:VAL60 4.1 43.4 1.0
N C:GLN61 4.2 45.5 1.0
N C:ALA57 4.2 40.8 1.0
C C:PRO58 4.3 41.3 1.0
N C:VAL60 4.3 42.8 1.0
CA C:ALA57 4.3 40.8 1.0
O C:PRO58 4.4 41.1 1.0
N C:GLY59 4.4 41.4 1.0
OE2 C:GLU54 4.5 38.2 1.0
N C:PRO58 4.5 40.6 1.0
N C:LEU55 4.5 39.6 1.0
CA C:PRO58 4.6 40.9 1.0
C C:VAL60 4.6 44.6 1.0
CA C:GLY59 4.6 41.6 1.0
CB C:GLU54 4.6 39.6 1.0
OD1 C:ASP485 4.7 34.1 1.0
CB C:ALA57 4.7 40.7 1.0
O61 C:DMU10 4.8 73.6 1.0
O C:MET53 4.8 40.1 1.0
CG C:GLN61 4.8 46.0 1.0
CA C:LEU55 4.8 39.7 1.0
CB C:GLN61 5.0 46.2 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: Sat Dec 12 04:23:37 2020

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