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Chlorine 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
Calcium (Ca) 2 atoms
Copper (Cu) 6 atoms

Chlorine Binding Sites:

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

Chlorine binding site 1 out of 2 in 3omn

Go back to Chlorine Binding Sites List in 3omn
Chlorine 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 Chlorine with other atoms in the Cl 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:Cl10

b:41.9
occ:1.00
O A:HOH711 3.1 35.4 1.0
O A:HOH714 3.2 60.4 1.0
N A:HIS26 3.3 42.7 1.0
N A:MET133 3.3 48.1 1.0
CD2 A:HIS26 3.7 42.4 1.0
CB A:HIS26 3.7 41.6 1.0
CA A:ALA132 3.8 48.9 1.0
O A:THR24 3.9 50.1 1.0
CA A:ASN25 3.9 45.9 1.0
CG A:HIS26 4.0 42.4 1.0
C A:ALA132 4.1 48.4 1.0
CA A:HIS26 4.1 42.1 1.0
CB A:ALA132 4.1 48.7 1.0
C A:ASN25 4.1 44.5 1.0
CB A:MET133 4.1 47.7 1.0
CG A:MET133 4.2 46.6 1.0
CG A:PRO136 4.3 48.7 1.0
CA A:MET133 4.3 47.6 1.0
ND2 A:ASN25 4.4 45.7 1.0
CB A:PRO136 4.4 48.6 1.0
C A:THR24 4.7 50.6 1.0
O A:MET133 4.7 47.8 1.0
CG A:ASN25 4.7 45.7 1.0
N A:ASN25 4.8 48.1 1.0
CB A:ASN25 4.9 45.9 1.0
NE2 A:HIS26 4.9 41.5 1.0
CA A:PRO136 5.0 48.6 1.0

Chlorine binding site 2 out of 2 in 3omn

Go back to Chlorine Binding Sites List in 3omn
Chlorine 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 Chlorine with other atoms in the Cl 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:Cl554

b:68.9
occ:1.00
N C:MET133 2.9 69.5 1.0
CA C:ALA132 3.5 69.7 1.0
CB C:ALA132 3.6 69.6 1.0
N C:HIS26 3.7 71.0 1.0
C C:ALA132 3.7 69.6 1.0
CD2 C:HIS26 3.8 70.9 1.0
CB C:MET133 3.8 69.5 1.0
CG C:MET133 3.8 69.4 1.0
CA C:MET133 3.9 69.6 1.0
CB C:HIS26 4.0 69.9 1.0
O C:THR24 4.0 75.8 1.0
CG C:PRO136 4.2 69.8 1.0
CG C:HIS26 4.2 70.5 1.0
CA C:ASN25 4.3 73.5 1.0
CB C:PRO136 4.4 69.8 1.0
CA C:HIS26 4.4 69.8 1.0
ND2 C:ASN25 4.4 74.5 1.0
O C:MET133 4.5 69.6 1.0
C C:ASN25 4.5 72.4 1.0
C C:MET133 4.7 69.7 1.0
O C:ALA132 4.9 69.7 1.0
CA C:PRO136 4.9 69.8 1.0
N C:ALA132 4.9 69.6 1.0
C C:THR24 5.0 76.0 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: Sun Jul 21 01:47:43 2024

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