Atomistry » Iron » PDB 4a9v-4b2y » 4ax3
Atomistry »
  Iron »
    PDB 4a9v-4b2y »
      4ax3 »

Iron in PDB 4ax3: Structure of Three-Domain Heme-Cu Nitrite Reductase From Ralstonia Pickettii at 1.6 A Resolution

Enzymatic activity of Structure of Three-Domain Heme-Cu Nitrite Reductase From Ralstonia Pickettii at 1.6 A Resolution

All present enzymatic activity of Structure of Three-Domain Heme-Cu Nitrite Reductase From Ralstonia Pickettii at 1.6 A Resolution:
1.7.2.1;

Protein crystallography data

The structure of Structure of Three-Domain Heme-Cu Nitrite Reductase From Ralstonia Pickettii at 1.6 A Resolution, PDB code: 4ax3 was solved by S.V.Antonyuk, H.Cong, R.R.Eady, S.S.Hasnain, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 25.00 / 1.60
Space group P 21 3
Cell size a, b, c (Å), α, β, γ (°) 185.812, 185.812, 185.812, 90.00, 90.00, 90.00
R / Rfree (%) 16.3 / 19.4

Other elements in 4ax3:

The structure of Structure of Three-Domain Heme-Cu Nitrite Reductase From Ralstonia Pickettii at 1.6 A Resolution also contains other interesting chemical elements:

Copper (Cu) 8 atoms

Iron Binding Sites:

The binding sites of Iron atom in the Structure of Three-Domain Heme-Cu Nitrite Reductase From Ralstonia Pickettii at 1.6 A Resolution (pdb code 4ax3). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 4 binding sites of Iron where determined in the Structure of Three-Domain Heme-Cu Nitrite Reductase From Ralstonia Pickettii at 1.6 A Resolution, PDB code: 4ax3:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in 4ax3

Go back to Iron Binding Sites List in 4ax3
Iron binding site 1 out of 4 in the Structure of Three-Domain Heme-Cu Nitrite Reductase From Ralstonia Pickettii at 1.6 A Resolution


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Structure of Three-Domain Heme-Cu Nitrite Reductase From Ralstonia Pickettii at 1.6 A Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe600

b:27.6
occ:1.00
 FE A:HEC600 0.0 27.6 1.0
NB A:HEC600 2.0 29.1 1.0
NE2 A:HIS368 2.0 26.8 1.0
ND A:HEC600 2.0 30.0 1.0
NC A:HEC600 2.1 23.9 1.0
NA A:HEC600 2.1 27.1 1.0
SD A:MET418 2.3 30.1 1.0
CE1 A:HIS368 3.0 28.9 1.0
C4B A:HEC600 3.0 29.7 1.0
C4C A:HEC600 3.0 26.8 1.0
C4D A:HEC600 3.0 30.6 1.0
CD2 A:HIS368 3.0 26.8 1.0
C1A A:HEC600 3.0 31.9 1.0
C1C A:HEC600 3.0 27.6 1.0
C1B A:HEC600 3.0 28.9 1.0
C4A A:HEC600 3.1 28.8 1.0
C1D A:HEC600 3.1 28.3 1.0
CE A:MET418 3.4 28.9 1.0
CHA A:HEC600 3.4 29.7 1.0
CG A:MET418 3.4 30.2 1.0
CHC A:HEC600 3.4 28.0 1.0
CHD A:HEC600 3.4 28.1 1.0
CHB A:HEC600 3.4 28.6 1.0
ND1 A:HIS368 4.1 27.5 1.0
CB A:MET418 4.2 30.4 1.0
CG A:HIS368 4.2 28.0 1.0
C3B A:HEC600 4.2 28.8 1.0
C2C A:HEC600 4.3 27.7 1.0
C3C A:HEC600 4.3 25.9 1.0
C2A A:HEC600 4.3 30.3 1.0
C3D A:HEC600 4.3 30.4 1.0
C3A A:HEC600 4.3 30.3 1.0
C2B A:HEC600 4.3 29.4 1.0
C2D A:HEC600 4.3 29.6 1.0

Iron binding site 2 out of 4 in 4ax3

Go back to Iron Binding Sites List in 4ax3
Iron binding site 2 out of 4 in the Structure of Three-Domain Heme-Cu Nitrite Reductase From Ralstonia Pickettii at 1.6 A Resolution


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Structure of Three-Domain Heme-Cu Nitrite Reductase From Ralstonia Pickettii at 1.6 A Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe600

b:23.8
occ:1.00
 FE B:HEC600 0.0 23.8 1.0
NB B:HEC600 1.9 23.8 1.0
NE2 B:HIS368 2.0 25.6 1.0
ND B:HEC600 2.0 25.5 1.0
NC B:HEC600 2.1 20.6 1.0
NA B:HEC600 2.1 21.1 1.0
SD B:MET418 2.2 24.6 1.0
CE1 B:HIS368 3.0 25.3 1.0
C4B B:HEC600 3.0 25.3 1.0
C4C B:HEC600 3.0 22.3 1.0
C1B B:HEC600 3.0 25.7 1.0
C4A B:HEC600 3.0 24.1 1.0
CD2 B:HIS368 3.0 24.2 1.0
C1C B:HEC600 3.1 25.5 1.0
C1A B:HEC600 3.1 26.3 1.0
C1D B:HEC600 3.1 24.4 1.0
C4D B:HEC600 3.1 24.6 1.0
CE B:MET418 3.3 23.6 1.0
CHC B:HEC600 3.4 24.0 1.0
CG B:MET418 3.4 24.3 1.0
CHD B:HEC600 3.4 24.9 1.0
CHB B:HEC600 3.4 24.1 1.0
CHA B:HEC600 3.4 25.6 1.0
ND1 B:HIS368 4.1 24.8 1.0
CB B:MET418 4.1 25.2 1.0
CG B:HIS368 4.2 26.2 1.0
C3B B:HEC600 4.2 24.3 1.0
C3C B:HEC600 4.2 22.9 1.0
C2B B:HEC600 4.2 27.2 1.0
C3A B:HEC600 4.3 25.7 1.0
C2C B:HEC600 4.3 23.4 1.0
C2A B:HEC600 4.3 24.4 1.0
C3D B:HEC600 4.3 24.9 1.0
C2D B:HEC600 4.3 25.1 1.0

Iron binding site 3 out of 4 in 4ax3

Go back to Iron Binding Sites List in 4ax3
Iron binding site 3 out of 4 in the Structure of Three-Domain Heme-Cu Nitrite Reductase From Ralstonia Pickettii at 1.6 A Resolution


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Structure of Three-Domain Heme-Cu Nitrite Reductase From Ralstonia Pickettii at 1.6 A Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Fe600

b:17.8
occ:1.00
 FE C:HEC600 0.0 17.8 1.0
NB C:HEC600 2.0 16.8 1.0
ND C:HEC600 2.0 19.2 1.0
NA C:HEC600 2.0 16.5 1.0
NC C:HEC600 2.0 14.7 1.0
NE2 C:HIS368 2.1 19.1 1.0
SD C:MET418 2.3 17.8 1.0
C4C C:HEC600 3.0 16.2 1.0
CE1 C:HIS368 3.0 21.1 1.0
C4A C:HEC600 3.0 17.1 1.0
C1C C:HEC600 3.0 16.6 1.0
C4B C:HEC600 3.0 16.3 1.0
C1B C:HEC600 3.1 14.9 1.0
C1A C:HEC600 3.1 20.2 1.0
C4D C:HEC600 3.1 19.7 1.0
C1D C:HEC600 3.1 17.7 1.0
CD2 C:HIS368 3.1 17.6 1.0
CG C:MET418 3.4 17.9 1.0
CHD C:HEC600 3.4 19.0 1.0
CHC C:HEC600 3.4 16.1 1.0
CE C:MET418 3.4 17.4 1.0
CHB C:HEC600 3.4 17.3 1.0
CHA C:HEC600 3.5 19.4 1.0
ND1 C:HIS368 4.2 18.9 1.0
CB C:MET418 4.2 17.5 1.0
CG C:HIS368 4.2 18.8 1.0
C3C C:HEC600 4.2 16.8 1.0
C2C C:HEC600 4.2 15.5 1.0
C3B C:HEC600 4.3 16.8 1.0
C2A C:HEC600 4.3 20.3 1.0
C3A C:HEC600 4.3 17.8 1.0
C2B C:HEC600 4.3 16.9 1.0
C3D C:HEC600 4.3 19.8 1.0
C2D C:HEC600 4.3 20.2 1.0

Iron binding site 4 out of 4 in 4ax3

Go back to Iron Binding Sites List in 4ax3
Iron binding site 4 out of 4 in the Structure of Three-Domain Heme-Cu Nitrite Reductase From Ralstonia Pickettii at 1.6 A Resolution


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Structure of Three-Domain Heme-Cu Nitrite Reductase From Ralstonia Pickettii at 1.6 A Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Fe600

b:25.9
occ:1.00
 FE D:HEC600 0.0 25.9 1.0
NC D:HEC600 2.0 23.4 1.0
NA D:HEC600 2.0 26.2 1.0
NE2 D:HIS368 2.0 28.4 1.0
NB D:HEC600 2.0 26.7 1.0
ND D:HEC600 2.1 27.2 1.0
SD D:MET418 2.4 26.3 1.0
CE1 D:HIS368 3.0 26.9 1.0
C4C D:HEC600 3.0 25.4 1.0
C4A D:HEC600 3.0 26.3 1.0
C1C D:HEC600 3.0 25.5 1.0
C4B D:HEC600 3.0 26.2 1.0
C1A D:HEC600 3.0 28.7 1.0
C1B D:HEC600 3.1 25.9 1.0
C4D D:HEC600 3.1 28.0 1.0
CD2 D:HIS368 3.1 25.7 1.0
C1D D:HEC600 3.1 26.1 1.0
CHC D:HEC600 3.4 25.2 1.0
CHA D:HEC600 3.4 27.5 1.0
CHB D:HEC600 3.4 28.2 1.0
CHD D:HEC600 3.4 25.2 1.0
CG D:MET418 3.5 25.8 1.0
CE D:MET418 3.5 27.4 1.0
ND1 D:HIS368 4.1 28.1 1.0
CG D:HIS368 4.2 26.0 1.0
CB D:MET418 4.2 27.3 1.0
C3C D:HEC600 4.2 24.2 1.0
C2C D:HEC600 4.2 24.1 1.0
C3B D:HEC600 4.2 25.5 1.0
C3A D:HEC600 4.2 28.1 1.0
C2A D:HEC600 4.3 28.8 1.0
C2B D:HEC600 4.3 25.9 1.0
C3D D:HEC600 4.3 27.8 1.0
C2D D:HEC600 4.3 27.4 1.0

Reference:

S.V.Antonyuk, C.Han, R.R.Eady, S.S.Hasnain. Structures of Protein-Protein Complexes Involved in Electron Transfer. Nature V. 496 123 2013.
ISSN: ESSN 1476-4687
PubMed: 23535590
DOI: 10.1038/NATURE11996
Page generated: Sun Aug 4 23:48:27 2024

Last articles

Zn in 9JYW
Zn in 9IR4
Zn in 9IR3
Zn in 9GMX
Zn in 9GMW
Zn in 9JEJ
Zn in 9ERF
Zn in 9ERE
Zn in 9EGV
Zn in 9EGW
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy