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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

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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

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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 Aug 4 12:18:16 2024

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