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Iron in PDB 3iq6: Crystal Structure of A Tetrameric Zn-Bound Cytochrome CB562 Complex with Covalently and Non-Covalently Stabilized Interfaces

Protein crystallography data

The structure of Crystal Structure of A Tetrameric Zn-Bound Cytochrome CB562 Complex with Covalently and Non-Covalently Stabilized Interfaces, PDB code: 3iq6 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 / 2.35
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 63.265, 76.770, 177.566, 90.00, 90.00, 90.00
R / Rfree (%) 22.8 / 29.6

Other elements in 3iq6:

The structure of Crystal Structure of A Tetrameric Zn-Bound Cytochrome CB562 Complex with Covalently and Non-Covalently Stabilized Interfaces also contains other interesting chemical elements:

Zinc (Zn) 8 atoms

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure of A Tetrameric Zn-Bound Cytochrome CB562 Complex with Covalently and Non-Covalently Stabilized Interfaces (pdb code 3iq6). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 8 binding sites of Iron where determined in the Crystal Structure of A Tetrameric Zn-Bound Cytochrome CB562 Complex with Covalently and Non-Covalently Stabilized Interfaces, PDB code: 3iq6:
Jump to Iron binding site number: 1; 2; 3; 4; 5; 6; 7; 8;

Iron binding site 1 out of 8 in 3iq6

Go back to Iron Binding Sites List in 3iq6
Iron binding site 1 out of 8 in the Crystal Structure of A Tetrameric Zn-Bound Cytochrome CB562 Complex with Covalently and Non-Covalently Stabilized Interfaces


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 A Tetrameric Zn-Bound Cytochrome CB562 Complex with Covalently and Non-Covalently Stabilized Interfaces within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe150

b:52.8
occ:1.00
FE A:HEM150 0.0 52.8 1.0
ND A:HEM150 1.8 60.4 1.0
NB A:HEM150 2.0 51.5 1.0
NC A:HEM150 2.0 55.1 1.0
NA A:HEM150 2.1 61.1 1.0
NE2 A:HIS102 2.1 49.9 1.0
SD A:MET7 2.1 49.1 1.0
C4D A:HEM150 2.9 62.0 1.0
C1D A:HEM150 2.9 61.4 1.0
CD2 A:HIS102 3.0 54.4 1.0
C4B A:HEM150 3.1 51.3 1.0
C4C A:HEM150 3.1 54.0 1.0
C1A A:HEM150 3.1 63.8 1.0
C1C A:HEM150 3.1 51.0 1.0
C1B A:HEM150 3.1 53.9 1.0
CE1 A:HIS102 3.1 54.4 1.0
C4A A:HEM150 3.2 60.7 1.0
CHD A:HEM150 3.3 59.5 1.0
CHA A:HEM150 3.3 64.1 1.0
CHC A:HEM150 3.4 53.5 1.0
CE A:MET7 3.5 50.4 1.0
CHB A:HEM150 3.5 57.7 1.0
CG A:MET7 3.6 54.3 1.0
C2D A:HEM150 4.1 61.9 1.0
C3D A:HEM150 4.1 62.7 1.0
CG A:HIS102 4.2 53.9 1.0
ND1 A:HIS102 4.2 50.3 1.0
C2C A:HEM150 4.3 50.6 1.0
C3C A:HEM150 4.3 51.7 1.0
C3B A:HEM150 4.3 51.7 1.0
C2B A:HEM150 4.3 51.8 1.0
C2A A:HEM150 4.4 68.0 1.0
CB A:MET7 4.4 50.4 1.0
C3A A:HEM150 4.4 66.3 1.0

Iron binding site 2 out of 8 in 3iq6

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Iron binding site 2 out of 8 in the Crystal Structure of A Tetrameric Zn-Bound Cytochrome CB562 Complex with Covalently and Non-Covalently Stabilized Interfaces


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 A Tetrameric Zn-Bound Cytochrome CB562 Complex with Covalently and Non-Covalently Stabilized Interfaces within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe150

b:29.2
occ:1.00
FE B:HEM150 0.0 29.2 1.0
NB B:HEM150 1.9 29.6 1.0
ND B:HEM150 2.0 31.7 1.0
NC B:HEM150 2.0 30.5 1.0
NE2 B:HIS102 2.0 29.2 1.0
NA B:HEM150 2.0 31.9 1.0
SD B:MET7 2.3 35.4 1.0
C4B B:HEM150 2.9 30.8 1.0
C1C B:HEM150 2.9 29.1 1.0
C4D B:HEM150 2.9 33.9 1.0
C1A B:HEM150 3.0 34.3 1.0
CE1 B:HIS102 3.0 25.0 1.0
CD2 B:HIS102 3.0 25.3 1.0
C1D B:HEM150 3.1 31.1 1.0
C1B B:HEM150 3.1 31.6 1.0
C4C B:HEM150 3.1 29.7 1.0
C4A B:HEM150 3.2 30.6 1.0
CHC B:HEM150 3.2 30.0 1.0
CHA B:HEM150 3.3 30.4 1.0
CG B:MET7 3.4 33.0 1.0
CE B:MET7 3.4 37.6 1.0
CHD B:HEM150 3.5 28.7 1.0
CHB B:HEM150 3.6 33.1 1.0
ND1 B:HIS102 4.1 29.8 1.0
CG B:HIS102 4.1 29.2 1.0
C3B B:HEM150 4.2 29.8 1.0
CB B:MET7 4.2 35.3 1.0
C2C B:HEM150 4.2 25.3 1.0
C3D B:HEM150 4.2 32.0 1.0
C2A B:HEM150 4.3 39.8 1.0
C2D B:HEM150 4.3 33.6 1.0
C2B B:HEM150 4.3 29.2 1.0
C3C B:HEM150 4.3 31.3 1.0
C3A B:HEM150 4.4 32.5 1.0

Iron binding site 3 out of 8 in 3iq6

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Iron binding site 3 out of 8 in the Crystal Structure of A Tetrameric Zn-Bound Cytochrome CB562 Complex with Covalently and Non-Covalently Stabilized Interfaces


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 A Tetrameric Zn-Bound Cytochrome CB562 Complex with Covalently and Non-Covalently Stabilized Interfaces within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Fe150

b:28.5
occ:1.00
FE C:HEM150 0.0 28.5 1.0
NC C:HEM150 1.9 19.8 1.0
NE2 C:HIS102 2.0 32.1 1.0
NA C:HEM150 2.0 30.7 1.0
ND C:HEM150 2.0 30.8 1.0
NB C:HEM150 2.0 23.7 1.0
SD C:MET7 2.2 35.9 1.0
CE1 C:HIS102 2.8 30.5 1.0
C1C C:HEM150 3.0 18.3 1.0
C4C C:HEM150 3.0 22.5 1.0
C1A C:HEM150 3.0 31.8 1.0
C1D C:HEM150 3.0 32.0 1.0
C4D C:HEM150 3.0 32.8 1.0
C4B C:HEM150 3.1 19.9 1.0
C4A C:HEM150 3.1 30.0 1.0
CD2 C:HIS102 3.1 29.9 1.0
C1B C:HEM150 3.1 22.3 1.0
CHD C:HEM150 3.4 26.3 1.0
CHC C:HEM150 3.4 16.2 1.0
CHA C:HEM150 3.4 32.0 1.0
CE C:MET7 3.4 32.7 1.0
CHB C:HEM150 3.4 27.3 1.0
CG C:MET7 3.6 35.6 1.0
ND1 C:HIS102 4.0 29.3 1.0
CG C:HIS102 4.1 25.5 1.0
C2C C:HEM150 4.2 19.7 1.0
C3C C:HEM150 4.3 22.7 1.0
C2A C:HEM150 4.3 32.8 1.0
C2D C:HEM150 4.3 33.8 1.0
C3D C:HEM150 4.3 38.1 1.0
C2B C:HEM150 4.3 19.9 1.0
C3B C:HEM150 4.3 17.2 1.0
C3A C:HEM150 4.3 33.6 1.0
NH1 C:ARG106 4.3 59.4 1.0
CB C:MET7 4.4 35.9 1.0

Iron binding site 4 out of 8 in 3iq6

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Iron binding site 4 out of 8 in the Crystal Structure of A Tetrameric Zn-Bound Cytochrome CB562 Complex with Covalently and Non-Covalently Stabilized Interfaces


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 A Tetrameric Zn-Bound Cytochrome CB562 Complex with Covalently and Non-Covalently Stabilized Interfaces within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Fe150

b:35.8
occ:1.00
FE D:HEM150 0.0 35.8 1.0
NB D:HEM150 1.9 38.1 1.0
NE2 D:HIS102 1.9 41.0 1.0
ND D:HEM150 2.0 35.6 1.0
NC D:HEM150 2.0 34.6 1.0
NA D:HEM150 2.1 41.1 1.0
SD D:MET7 2.4 36.1 1.0
CE1 D:HIS102 2.7 37.4 1.0
C4B D:HEM150 2.9 38.9 1.0
C1B D:HEM150 2.9 42.1 1.0
C1C D:HEM150 3.0 32.2 1.0
C1D D:HEM150 3.0 39.0 1.0
C4D D:HEM150 3.0 42.0 1.0
CD2 D:HIS102 3.0 35.9 1.0
C4C D:HEM150 3.1 35.0 1.0
C4A D:HEM150 3.1 41.0 1.0
C1A D:HEM150 3.2 42.8 1.0
CHC D:HEM150 3.3 36.5 1.0
CHB D:HEM150 3.4 43.0 1.0
CHD D:HEM150 3.4 36.6 1.0
CHA D:HEM150 3.5 42.1 1.0
CG D:MET7 3.5 36.0 1.0
CE D:MET7 3.5 37.8 1.0
ND1 D:HIS102 3.9 34.7 1.0
CG D:HIS102 4.1 39.1 1.0
C2B D:HEM150 4.2 42.6 1.0
C3B D:HEM150 4.2 40.9 1.0
C2C D:HEM150 4.2 33.0 1.0
C2D D:HEM150 4.3 38.5 1.0
C3D D:HEM150 4.3 40.2 1.0
C3C D:HEM150 4.3 34.5 1.0
CB D:MET7 4.3 36.6 1.0
C3A D:HEM150 4.4 44.7 1.0
C2A D:HEM150 4.5 45.7 1.0

Iron binding site 5 out of 8 in 3iq6

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Iron binding site 5 out of 8 in the Crystal Structure of A Tetrameric Zn-Bound Cytochrome CB562 Complex with Covalently and Non-Covalently Stabilized Interfaces


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 5 of Crystal Structure of A Tetrameric Zn-Bound Cytochrome CB562 Complex with Covalently and Non-Covalently Stabilized Interfaces within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Fe150

b:24.6
occ:1.00
FE E:HEM150 0.0 24.6 1.0
ND E:HEM150 1.8 25.4 1.0
NC E:HEM150 1.9 22.2 1.0
NA E:HEM150 1.9 15.2 1.0
NE2 E:HIS102 2.1 37.4 1.0
NB E:HEM150 2.1 17.7 1.0
SD E:MET7 2.3 28.6 1.0
C4D E:HEM150 2.8 28.0 1.0
C1A E:HEM150 2.8 19.5 1.0
C1C E:HEM150 2.9 23.0 1.0
C1D E:HEM150 3.0 23.7 1.0
C4C E:HEM150 3.0 26.0 1.0
CE1 E:HIS102 3.0 29.6 1.0
C4B E:HEM150 3.1 22.2 1.0
C4A E:HEM150 3.1 19.8 1.0
CD2 E:HIS102 3.1 33.2 1.0
CHA E:HEM150 3.2 21.0 1.0
C1B E:HEM150 3.2 20.0 1.0
CE E:MET7 3.3 25.6 1.0
CHC E:HEM150 3.3 21.0 1.0
CHD E:HEM150 3.4 23.8 1.0
CG E:MET7 3.4 25.6 1.0
CHB E:HEM150 3.6 22.3 1.0
C3D E:HEM150 4.0 28.0 1.0
C2D E:HEM150 4.1 26.3 1.0
C2A E:HEM150 4.2 21.8 1.0
ND1 E:HIS102 4.2 37.4 1.0
C3C E:HEM150 4.2 27.6 1.0
C2C E:HEM150 4.2 22.8 1.0
CG E:HIS102 4.2 38.5 1.0
CB E:MET7 4.2 29.3 1.0
C3A E:HEM150 4.3 24.1 1.0
C3B E:HEM150 4.4 21.9 1.0
C2B E:HEM150 4.4 23.7 1.0
NH1 E:ARG106 4.6 38.1 1.0

Iron binding site 6 out of 8 in 3iq6

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Iron binding site 6 out of 8 in the Crystal Structure of A Tetrameric Zn-Bound Cytochrome CB562 Complex with Covalently and Non-Covalently Stabilized Interfaces


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 6 of Crystal Structure of A Tetrameric Zn-Bound Cytochrome CB562 Complex with Covalently and Non-Covalently Stabilized Interfaces within 5.0Å range:
probe atom residue distance (Å) B Occ
F:Fe150

b:32.6
occ:1.00
FE F:HEM150 0.0 32.6 1.0
ND F:HEM150 1.8 35.8 1.0
NC F:HEM150 1.9 31.0 1.0
NE2 F:HIS102 2.0 21.2 1.0
NA F:HEM150 2.1 40.1 1.0
NB F:HEM150 2.1 30.9 1.0
SD F:MET7 2.3 37.9 1.0
C1D F:HEM150 2.8 36.3 1.0
C4D F:HEM150 2.9 38.5 1.0
C4C F:HEM150 2.9 32.1 1.0
C1C F:HEM150 3.0 30.5 1.0
CE1 F:HIS102 3.0 19.3 1.0
CD2 F:HIS102 3.1 22.0 1.0
C1A F:HEM150 3.1 39.4 1.0
C4B F:HEM150 3.1 30.5 1.0
C4A F:HEM150 3.1 39.9 1.0
C1B F:HEM150 3.2 30.3 1.0
CHD F:HEM150 3.2 30.1 1.0
CE F:MET7 3.3 37.6 1.0
CG F:MET7 3.4 42.0 1.0
CHA F:HEM150 3.4 40.2 1.0
CHC F:HEM150 3.4 28.4 1.0
CHB F:HEM150 3.5 36.0 1.0
C2D F:HEM150 4.1 35.9 1.0
ND1 F:HIS102 4.1 23.1 1.0
C3D F:HEM150 4.2 38.0 1.0
CG F:HIS102 4.2 23.7 1.0
CB F:MET7 4.2 45.3 1.0
C2C F:HEM150 4.2 29.4 1.0
C3C F:HEM150 4.2 29.7 1.0
C3A F:HEM150 4.4 40.0 1.0
C3B F:HEM150 4.4 30.4 1.0
C2A F:HEM150 4.4 44.9 1.0
C2B F:HEM150 4.4 31.4 1.0
NH1 F:ARG106 4.7 54.6 1.0

Iron binding site 7 out of 8 in 3iq6

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Iron binding site 7 out of 8 in the Crystal Structure of A Tetrameric Zn-Bound Cytochrome CB562 Complex with Covalently and Non-Covalently Stabilized Interfaces


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 7 of Crystal Structure of A Tetrameric Zn-Bound Cytochrome CB562 Complex with Covalently and Non-Covalently Stabilized Interfaces within 5.0Å range:
probe atom residue distance (Å) B Occ
G:Fe150

b:53.4
occ:1.00
FE G:HEM150 0.0 53.4 1.0
NB G:HEM150 1.9 53.0 1.0
NE2 G:HIS102 2.0 45.5 1.0
NC G:HEM150 2.0 56.4 1.0
NA G:HEM150 2.0 58.9 1.0
ND G:HEM150 2.0 61.4 1.0
SD G:MET7 2.2 52.8 1.0
C4B G:HEM150 2.9 51.4 1.0
C1C G:HEM150 2.9 53.7 1.0
CE1 G:HIS102 2.9 49.1 1.0
C1A G:HEM150 3.0 60.2 1.0
CD2 G:HIS102 3.0 49.8 1.0
C4D G:HEM150 3.0 63.5 1.0
C1B G:HEM150 3.0 52.1 1.0
C4A G:HEM150 3.1 57.7 1.0
C4C G:HEM150 3.1 57.0 1.0
C1D G:HEM150 3.2 62.1 1.0
CHC G:HEM150 3.2 51.3 1.0
CHA G:HEM150 3.3 61.1 1.0
CHB G:HEM150 3.4 53.5 1.0
CE G:MET7 3.4 50.0 1.0
CHD G:HEM150 3.5 60.6 1.0
CG G:MET7 3.6 50.2 1.0
ND1 G:HIS102 4.1 48.7 1.0
CG G:HIS102 4.1 50.5 1.0
C3B G:HEM150 4.2 50.0 1.0
C2C G:HEM150 4.2 53.9 1.0
C2B G:HEM150 4.2 52.7 1.0
C2A G:HEM150 4.3 63.8 1.0
C3A G:HEM150 4.3 60.7 1.0
C3C G:HEM150 4.3 56.0 1.0
C3D G:HEM150 4.3 65.2 1.0
CB G:MET7 4.4 52.8 1.0
C2D G:HEM150 4.4 63.0 1.0

Iron binding site 8 out of 8 in 3iq6

Go back to Iron Binding Sites List in 3iq6
Iron binding site 8 out of 8 in the Crystal Structure of A Tetrameric Zn-Bound Cytochrome CB562 Complex with Covalently and Non-Covalently Stabilized Interfaces


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 8 of Crystal Structure of A Tetrameric Zn-Bound Cytochrome CB562 Complex with Covalently and Non-Covalently Stabilized Interfaces within 5.0Å range:
probe atom residue distance (Å) B Occ
H:Fe150

b:35.8
occ:1.00
FE H:HEM150 0.0 35.8 1.0
ND H:HEM150 1.8 36.5 1.0
NA H:HEM150 1.9 40.4 1.0
NE2 H:HIS102 2.1 37.4 1.0
NB H:HEM150 2.1 32.5 1.0
NC H:HEM150 2.1 35.0 1.0
SD H:MET7 2.3 42.7 1.0
C4D H:HEM150 2.8 38.7 1.0
C1A H:HEM150 2.9 42.4 1.0
C1D H:HEM150 2.9 39.5 1.0
C4A H:HEM150 3.0 41.9 1.0
CE1 H:HIS102 3.0 41.4 1.0
CD2 H:HIS102 3.1 40.4 1.0
C1B H:HEM150 3.1 37.7 1.0
C4C H:HEM150 3.1 38.9 1.0
C4B H:HEM150 3.2 34.0 1.0
CHA H:HEM150 3.2 41.0 1.0
C1C H:HEM150 3.2 33.4 1.0
CHD H:HEM150 3.4 38.7 1.0
CHB H:HEM150 3.4 37.2 1.0
CG H:MET7 3.5 42.3 1.0
CHC H:HEM150 3.5 33.9 1.0
CE H:MET7 3.6 46.3 1.0
C3D H:HEM150 4.1 40.5 1.0
ND1 H:HIS102 4.1 39.2 1.0
C2D H:HEM150 4.1 41.7 1.0
C2A H:HEM150 4.2 46.5 1.0
C3A H:HEM150 4.2 42.6 1.0
CB H:MET7 4.2 41.1 1.0
CG H:HIS102 4.2 42.2 1.0
C2B H:HEM150 4.4 38.2 1.0
C3B H:HEM150 4.4 33.6 1.0
C3C H:HEM150 4.4 35.6 1.0
C2C H:HEM150 4.5 38.0 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 12:18:18 2024

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