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Iron in PDB 6hih: Cytochrome C Prime Beta From Methylococcus Capsulatus (Bath)

Protein crystallography data

The structure of Cytochrome C Prime Beta From Methylococcus Capsulatus (Bath), PDB code: 6hih was solved by H.Adams, T.M.Chicano, M.A.Hough, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 61.20 / 1.60
Space group P 21 3
Cell size a, b, c (Å), α, β, γ (°) 105.960, 105.960, 105.960, 90.00, 90.00, 90.00
R / Rfree (%) 17.7 / 20.2

Other elements in 6hih:

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

Zinc (Zn) 2 atoms

Iron Binding Sites:

The binding sites of Iron atom in the Cytochrome C Prime Beta From Methylococcus Capsulatus (Bath) (pdb code 6hih). 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), PDB code: 6hih:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in 6hih

Go back to Iron Binding Sites List in 6hih
Iron binding site 1 out of 2 in the Cytochrome C Prime Beta From Methylococcus Capsulatus (Bath)


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) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe203

b:23.8
occ:1.00
FE A:HEC203 0.0 23.8 1.0
NA A:HEC203 2.0 21.1 1.0
ND A:HEC203 2.0 24.4 1.0
NC A:HEC203 2.0 24.4 1.0
NB A:HEC203 2.0 23.3 1.0
NE2 A:HIS123 2.1 23.7 1.0
C1A A:HEC203 3.0 20.7 1.0
CE1 A:HIS123 3.0 25.4 1.0
C1B A:HEC203 3.0 24.6 1.0
C1D A:HEC203 3.0 25.8 1.0
C1C A:HEC203 3.1 26.8 1.0
C4B A:HEC203 3.1 25.8 1.0
C4D A:HEC203 3.1 21.6 1.0
C4C A:HEC203 3.1 26.7 1.0
C4A A:HEC203 3.1 24.0 1.0
CD2 A:HIS123 3.1 24.1 1.0
CHC A:HEC203 3.4 27.4 1.0
CHD A:HEC203 3.4 27.9 1.0
CHB A:HEC203 3.4 22.5 1.0
CHA A:HEC203 3.4 20.1 1.0
CE2 A:PHE32 4.0 59.0 1.0
ND1 A:HIS123 4.2 24.8 1.0
CZ A:PHE32 4.2 61.1 1.0
C2B A:HEC203 4.3 25.9 1.0
C2D A:HEC203 4.3 24.0 1.0
C2A A:HEC203 4.3 20.7 1.0
CG A:HIS123 4.3 26.3 1.0
C3A A:HEC203 4.3 21.3 1.0
C2C A:HEC203 4.3 29.1 1.0
C3D A:HEC203 4.3 22.7 1.0
C3C A:HEC203 4.3 29.7 1.0
C3B A:HEC203 4.3 26.5 1.0
CE1 A:PHE133 4.7 27.4 1.0
CD1 A:PHE133 4.9 25.9 1.0

Iron binding site 2 out of 2 in 6hih

Go back to Iron Binding Sites List in 6hih
Iron binding site 2 out of 2 in the Cytochrome C Prime Beta From Methylococcus Capsulatus (Bath)


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) within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe201

b:24.9
occ:1.00
FE B:HEC201 0.0 24.9 1.0
ND B:HEC201 2.0 25.3 1.0
NA B:HEC201 2.0 21.9 1.0
NB B:HEC201 2.1 25.1 1.0
NE2 B:HIS123 2.1 22.8 1.0
NC B:HEC201 2.1 26.4 1.0
C4D B:HEC201 3.0 23.9 1.0
C4A B:HEC201 3.0 22.6 1.0
C1B B:HEC201 3.0 25.2 1.0
C1A B:HEC201 3.1 20.8 1.0
CE1 B:HIS123 3.1 25.2 1.0
C1C B:HEC201 3.1 26.5 1.0
C4C B:HEC201 3.1 25.4 1.0
C1D B:HEC201 3.1 24.7 1.0
C4B B:HEC201 3.1 25.9 1.0
CD2 B:HIS123 3.2 22.9 1.0
CHB B:HEC201 3.4 22.4 1.0
CHA B:HEC201 3.4 22.6 1.0
CHC B:HEC201 3.4 26.9 1.0
CHD B:HEC201 3.5 25.4 1.0
CE2 B:PHE32 3.9 42.0 1.0
ND1 B:HIS123 4.2 24.8 1.0
C2A B:HEC201 4.2 21.3 1.0
C3A B:HEC201 4.2 22.2 1.0
C2C B:HEC201 4.3 27.1 1.0
C3D B:HEC201 4.3 23.2 1.0
CG B:HIS123 4.3 25.8 1.0
C2B B:HEC201 4.3 26.5 1.0
C3C B:HEC201 4.3 27.3 1.0
C2D B:HEC201 4.3 24.7 1.0
C3B B:HEC201 4.3 26.8 1.0
CZ B:PHE32 4.5 39.8 1.0
CE2 B:PHE133 4.7 26.9 1.0
CD2 B:PHE32 4.9 42.0 1.0
CD2 B:PHE133 4.9 24.4 1.0

Reference:

H.R.Adams, C.Krewson, J.E.Vardanega, S.Fujii, T.Moreno, Y.Sambongi, D.Svistunenko, J.Paps, C.R.Andrew, M.A.Hough. One Fold, Two Functions: Cytochrome P460 and Cytochromec'-Beta From the Methanotrophmethylococcus Capsulatus(Bath). Chem Sci V. 10 3031 2019.
ISSN: ISSN 2041-6520
PubMed: 30996884
DOI: 10.1039/C8SC05210G
Page generated: Sun Dec 13 16:28:32 2020

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