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Iron in PDB 7zvz: Cytochrome C Prime Beta From Methylococcus Capsulatus (Bath): Chemically Reduced Ferrous Form

Protein crystallography data

The structure of Cytochrome C Prime Beta From Methylococcus Capsulatus (Bath): Chemically Reduced Ferrous Form, PDB code: 7zvz was solved by H.R.Adams, M.A.Hough, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 37.35 / 1.68
Space group P 21 3
Cell size a, b, c (Å), α, β, γ (°) 105.56, 105.56, 105.56, 90, 90, 90
R / Rfree (%) 19.2 / 22.8

Other elements in 7zvz:

The structure of Cytochrome C Prime Beta From Methylococcus Capsulatus (Bath): Chemically Reduced Ferrous Form also contains other interesting chemical elements:

Zinc (Zn) 1 atom

Iron Binding Sites:

The binding sites of Iron atom in the Cytochrome C Prime Beta From Methylococcus Capsulatus (Bath): Chemically Reduced Ferrous Form (pdb code 7zvz). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Cytochrome C Prime Beta From Methylococcus Capsulatus (Bath): Chemically Reduced Ferrous Form, PDB code: 7zvz:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in 7zvz

Go back to Iron Binding Sites List in 7zvz
Iron binding site 1 out of 2 in the Cytochrome C Prime Beta From Methylococcus Capsulatus (Bath): Chemically Reduced Ferrous Form


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Cytochrome C Prime Beta From Methylococcus Capsulatus (Bath): Chemically Reduced Ferrous Form within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe201

b:27.3
occ:1.00
FE A:HEC201 0.0 27.3 1.0
NA A:HEC201 2.0 26.3 1.0
NC A:HEC201 2.1 29.6 1.0
ND A:HEC201 2.1 26.9 1.0
NB A:HEC201 2.1 26.9 1.0
NE2 A:HIS123 2.1 27.1 1.0
C1A A:HEC201 3.0 25.4 1.0
C4B A:HEC201 3.0 29.1 1.0
CE1 A:HIS123 3.0 26.8 1.0
C4C A:HEC201 3.1 31.6 1.0
C1D A:HEC201 3.1 30.7 1.0
C1B A:HEC201 3.1 29.2 1.0
C1C A:HEC201 3.1 33.2 1.0
C4D A:HEC201 3.1 26.0 1.0
C4A A:HEC201 3.1 26.1 1.0
CD2 A:HIS123 3.2 26.5 1.0
CHD A:HEC201 3.4 31.8 1.0
CHC A:HEC201 3.4 31.3 1.0
CHA A:HEC201 3.4 23.6 1.0
CHB A:HEC201 3.5 26.0 1.0
ND1 A:HIS123 4.2 28.8 1.0
CG A:HIS123 4.3 29.5 1.0
C2A A:HEC201 4.3 24.5 1.0
C2D A:HEC201 4.3 29.8 1.0
C3A A:HEC201 4.4 24.6 1.0
C3B A:HEC201 4.4 29.6 1.0
C3D A:HEC201 4.4 28.8 1.0
C3C A:HEC201 4.4 31.9 1.0
C2C A:HEC201 4.4 31.9 1.0
C2B A:HEC201 4.4 28.9 1.0
CE1 A:PHE133 4.9 32.4 1.0
CD1 A:PHE133 5.0 29.7 1.0

Iron binding site 2 out of 2 in 7zvz

Go back to Iron Binding Sites List in 7zvz
Iron binding site 2 out of 2 in the Cytochrome C Prime Beta From Methylococcus Capsulatus (Bath): Chemically Reduced Ferrous Form


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Cytochrome C Prime Beta From Methylococcus Capsulatus (Bath): Chemically Reduced Ferrous Form within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe201

b:28.4
occ:1.00
FE B:HEC201 0.0 28.4 1.0
ND B:HEC201 2.0 30.1 1.0
NA B:HEC201 2.0 27.7 1.0
NB B:HEC201 2.1 29.4 1.0
NC B:HEC201 2.1 30.1 1.0
NE2 B:HIS123 2.1 29.7 1.0
C4D B:HEC201 3.0 27.8 1.0
C1A B:HEC201 3.0 27.1 1.0
C4A B:HEC201 3.1 28.3 1.0
C1D B:HEC201 3.1 30.7 1.0
C4C B:HEC201 3.1 31.4 1.0
C1B B:HEC201 3.1 29.4 1.0
C4B B:HEC201 3.1 30.1 1.0
C1C B:HEC201 3.1 29.8 1.0
CE1 B:HIS123 3.1 30.6 1.0
CD2 B:HIS123 3.2 28.0 1.0
CHA B:HEC201 3.4 24.9 1.0
CHD B:HEC201 3.5 30.4 1.0
CHC B:HEC201 3.5 30.8 1.0
CHB B:HEC201 3.5 29.9 1.0
CE2 B:PHE32 3.9 63.2 1.0
ND1 B:HIS123 4.2 29.5 1.0
CG B:HIS123 4.3 32.2 1.0
C3D B:HEC201 4.3 27.9 1.0
C2A B:HEC201 4.3 25.9 1.0
C2D B:HEC201 4.4 27.9 1.0
C3A B:HEC201 4.4 26.7 1.0
C3B B:HEC201 4.4 33.5 1.0
C3C B:HEC201 4.4 32.2 1.0
C2C B:HEC201 4.4 29.6 1.0
C2B B:HEC201 4.4 29.3 1.0
CZ B:PHE32 4.5 60.9 1.0
CE2 B:PHE133 4.8 32.1 1.0
CD2 B:PHE133 4.9 29.2 1.0
CD2 B:PHE32 5.0 63.5 1.0

Reference:

H.R.Adams, R.W.Strange, D.A.Svistunenko, C.R.Andrew, M.A.Hough. Cytochrome C Prime Beta From Methylococcus Capsulatus (Bath): Chemically Reduced Ferrous Form To Be Published.
Page generated: Fri Aug 9 15:30:43 2024

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