Atomistry » Iron » PDB 3i9t-3j7b » 3iq5
Atomistry »
  Iron »
    PDB 3i9t-3j7b »
      3iq5 »

Iron in PDB 3iq5: Crystal Structure of An Engineered Metal-Free Tetrameric Cytochrome CB562 Complex Templated By Zn-Coordination

Protein crystallography data

The structure of Crystal Structure of An Engineered Metal-Free Tetrameric Cytochrome CB562 Complex Templated By Zn-Coordination, PDB code: 3iq5 was solved by J.N.Brodin, F.A.Tezcan, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 50.00 / 2.05
Space group I 41
Cell size a, b, c (Å), α, β, γ (°) 69.153, 69.153, 186.935, 90.00, 90.00, 90.00
R / Rfree (%) 22.9 / 27.7

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure of An Engineered Metal-Free Tetrameric Cytochrome CB562 Complex Templated By Zn-Coordination (pdb code 3iq5). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 4 binding sites of Iron where determined in the Crystal Structure of An Engineered Metal-Free Tetrameric Cytochrome CB562 Complex Templated By Zn-Coordination, PDB code: 3iq5:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in 3iq5

Go back to Iron Binding Sites List in 3iq5
Iron binding site 1 out of 4 in the Crystal Structure of An Engineered Metal-Free Tetrameric Cytochrome CB562 Complex Templated By Zn-Coordination


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Crystal Structure of An Engineered Metal-Free Tetrameric Cytochrome CB562 Complex Templated By Zn-Coordination within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe150

b:17.8
occ:1.00
FE A:HEM150 0.0 17.8 1.0
ND A:HEM150 1.9 17.1 1.0
NB A:HEM150 2.0 16.9 1.0
NC A:HEM150 2.0 17.7 1.0
NA A:HEM150 2.1 18.3 1.0
NE2 A:HIS102 2.1 14.3 1.0
SD A:MET7 2.2 19.6 1.0
C4B A:HEM150 3.0 20.8 1.0
C1C A:HEM150 3.0 18.9 1.0
C1D A:HEM150 3.0 18.8 1.0
C4D A:HEM150 3.0 21.9 1.0
CD2 A:HIS102 3.0 19.0 1.0
C1A A:HEM150 3.1 19.2 1.0
C4C A:HEM150 3.1 18.2 1.0
C1B A:HEM150 3.1 16.8 1.0
CE1 A:HIS102 3.1 19.1 1.0
C4A A:HEM150 3.1 18.1 1.0
CHC A:HEM150 3.3 16.6 1.0
CE A:MET7 3.3 18.1 1.0
CG A:MET7 3.4 17.0 1.0
CHD A:HEM150 3.4 13.4 1.0
CHA A:HEM150 3.4 18.9 1.0
CHB A:HEM150 3.5 14.6 1.0
CG A:HIS102 4.2 20.2 1.0
ND1 A:HIS102 4.2 18.0 1.0
CB A:MET7 4.2 18.6 1.0
C2D A:HEM150 4.2 16.7 1.0
C3B A:HEM150 4.3 19.3 1.0
C2B A:HEM150 4.3 13.9 1.0
C3D A:HEM150 4.3 20.9 1.0
C2C A:HEM150 4.3 16.9 1.0
C2A A:HEM150 4.3 18.3 1.0
C3A A:HEM150 4.4 19.4 1.0
C3C A:HEM150 4.4 19.4 1.0

Iron binding site 2 out of 4 in 3iq5

Go back to Iron Binding Sites List in 3iq5
Iron binding site 2 out of 4 in the Crystal Structure of An Engineered Metal-Free Tetrameric Cytochrome CB562 Complex Templated By Zn-Coordination


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Crystal Structure of An Engineered Metal-Free Tetrameric Cytochrome CB562 Complex Templated By Zn-Coordination within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe150

b:19.0
occ:1.00
FE B:HEM150 0.0 19.0 1.0
ND B:HEM150 1.9 14.3 1.0
NA B:HEM150 2.0 21.0 1.0
NB B:HEM150 2.0 19.5 1.0
NC B:HEM150 2.1 17.9 1.0
NE2 B:HIS102 2.1 18.4 1.0
SD B:MET7 2.3 22.0 1.0
C4D B:HEM150 3.0 20.3 1.0
C1A B:HEM150 3.0 25.6 1.0
C1D B:HEM150 3.0 18.4 1.0
CD2 B:HIS102 3.0 20.5 1.0
C4B B:HEM150 3.0 19.2 1.0
C1C B:HEM150 3.1 16.5 1.0
C1B B:HEM150 3.1 24.1 1.0
CE1 B:HIS102 3.1 20.7 1.0
C4A B:HEM150 3.1 24.4 1.0
C4C B:HEM150 3.1 17.7 1.0
CE B:MET7 3.3 18.0 1.0
CHA B:HEM150 3.4 16.2 1.0
CHC B:HEM150 3.4 15.9 1.0
CG B:MET7 3.4 19.1 1.0
CHD B:HEM150 3.4 17.6 1.0
CHB B:HEM150 3.5 18.0 1.0
ND1 B:HIS102 4.2 16.9 1.0
CG B:HIS102 4.2 21.0 1.0
CB B:MET7 4.2 17.6 1.0
C3D B:HEM150 4.3 19.4 1.0
C2D B:HEM150 4.3 21.5 1.0
C2A B:HEM150 4.3 26.8 1.0
C2B B:HEM150 4.3 20.4 1.0
C3B B:HEM150 4.3 21.1 1.0
C3A B:HEM150 4.3 24.9 1.0
C2C B:HEM150 4.4 14.3 1.0
C3C B:HEM150 4.4 21.4 1.0
NH1 B:ARG106 4.9 41.1 1.0
CA B:MET7 5.0 20.2 1.0

Iron binding site 3 out of 4 in 3iq5

Go back to Iron Binding Sites List in 3iq5
Iron binding site 3 out of 4 in the Crystal Structure of An Engineered Metal-Free Tetrameric Cytochrome CB562 Complex Templated By Zn-Coordination


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Crystal Structure of An Engineered Metal-Free Tetrameric Cytochrome CB562 Complex Templated By Zn-Coordination within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Fe150

b:33.7
occ:1.00
FE C:HEM150 0.0 33.7 1.0
NE2 C:HIS102 1.9 21.1 1.0
NA C:HEM150 2.0 35.6 1.0
NB C:HEM150 2.0 29.9 1.0
ND C:HEM150 2.0 32.9 1.0
NC C:HEM150 2.1 30.2 1.0
SD C:MET7 2.2 33.3 1.0
CE1 C:HIS102 2.8 28.0 1.0
C4B C:HEM150 3.0 33.3 1.0
CD2 C:HIS102 3.0 27.0 1.0
C1A C:HEM150 3.0 36.7 1.0
C4D C:HEM150 3.0 35.2 1.0
C1C C:HEM150 3.0 29.7 1.0
C4A C:HEM150 3.0 35.9 1.0
C1B C:HEM150 3.1 34.3 1.0
C1D C:HEM150 3.2 33.1 1.0
C4C C:HEM150 3.2 29.1 1.0
CHC C:HEM150 3.3 28.1 1.0
CHA C:HEM150 3.3 33.8 1.0
CHB C:HEM150 3.4 33.2 1.0
CG C:MET7 3.5 37.9 1.0
CE C:MET7 3.5 30.9 1.0
CHD C:HEM150 3.6 30.7 1.0
ND1 C:HIS102 3.9 28.2 1.0
CG C:HIS102 4.1 26.4 1.0
CB C:MET7 4.2 35.5 1.0
C3B C:HEM150 4.3 34.4 1.0
C3A C:HEM150 4.3 39.5 1.0
C2B C:HEM150 4.3 32.0 1.0
C2A C:HEM150 4.3 36.7 1.0
C3D C:HEM150 4.3 36.1 1.0
C2C C:HEM150 4.4 24.7 1.0
C2D C:HEM150 4.4 34.4 1.0
C3C C:HEM150 4.4 27.9 1.0
CA C:MET7 4.9 40.1 1.0

Iron binding site 4 out of 4 in 3iq5

Go back to Iron Binding Sites List in 3iq5
Iron binding site 4 out of 4 in the Crystal Structure of An Engineered Metal-Free Tetrameric Cytochrome CB562 Complex Templated By Zn-Coordination


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Crystal Structure of An Engineered Metal-Free Tetrameric Cytochrome CB562 Complex Templated By Zn-Coordination within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Fe150

b:38.2
occ:1.00
FE D:HEM150 0.0 38.2 1.0
NB D:HEM150 1.9 34.7 1.0
NE2 D:HIS102 1.9 27.0 1.0
NC D:HEM150 2.0 32.2 1.0
ND D:HEM150 2.1 38.6 1.0
NA D:HEM150 2.1 40.9 1.0
SD D:MET7 2.3 44.5 1.0
CE1 D:HIS102 2.9 31.4 1.0
C4B D:HEM150 2.9 37.5 1.0
CD2 D:HIS102 2.9 31.9 1.0
C1C D:HEM150 3.0 34.9 1.0
C1B D:HEM150 3.0 40.6 1.0
C4A D:HEM150 3.1 41.7 1.0
C4C D:HEM150 3.1 34.4 1.0
C1D D:HEM150 3.1 40.7 1.0
C4D D:HEM150 3.1 41.4 1.0
C1A D:HEM150 3.1 41.8 1.0
CHC D:HEM150 3.3 34.4 1.0
CE D:MET7 3.3 42.1 1.0
CHB D:HEM150 3.4 40.5 1.0
CHD D:HEM150 3.5 34.4 1.0
CHA D:HEM150 3.5 40.2 1.0
CG D:MET7 3.6 41.5 1.0
ND1 D:HIS102 4.0 29.4 1.0
CG D:HIS102 4.0 35.1 1.0
C3B D:HEM150 4.2 35.4 1.0
C2B D:HEM150 4.2 37.1 1.0
C2C D:HEM150 4.3 33.0 1.0
C3A D:HEM150 4.3 43.0 1.0
C3C D:HEM150 4.4 31.5 1.0
C2D D:HEM150 4.4 40.6 1.0
C3D D:HEM150 4.4 43.6 1.0
C2A D:HEM150 4.4 46.5 1.0
CB D:MET7 4.5 41.4 1.0

Reference:

J.D.Brodin, A.Medina-Morales, T.Ni, E.N.Salgado, X.I.Ambroggio, F.A.Tezcan. Evolution of Metal Selectivity in Templated Protein Interfaces. J.Am.Chem.Soc. V. 132 8610 2010.
ISSN: ISSN 0002-7863
PubMed: 20515031
DOI: 10.1021/JA910844N
Page generated: Sun Dec 13 15:08:53 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