Atomistry » Magnesium » PDB 3ohb-3otb » 3om3
Atomistry »
  Magnesium »
    PDB 3ohb-3otb »
      3om3 »

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: Mon Dec 14 08:36:24 2020

Last articles

Zn in 8WB0
Zn in 8WAX
Zn in 8WAU
Zn in 8WAZ
Zn in 8WAY
Zn in 8WAV
Zn in 8WAW
Zn in 8WAT
Zn in 8W7M
Zn in 8WD3
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy