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Iron in PDB 9gdf: Chloride Bound Structure of Oxidized BA3-Type Cytochrome C Oxidase Confirmed By Single-Wavelength Anomalous Diffraction

Enzymatic activity of Chloride Bound Structure of Oxidized BA3-Type Cytochrome C Oxidase Confirmed By Single-Wavelength Anomalous Diffraction

All present enzymatic activity of Chloride Bound Structure of Oxidized BA3-Type Cytochrome C Oxidase Confirmed By Single-Wavelength Anomalous Diffraction:
1.9.3.1; 7.1.1.9;

Protein crystallography data

The structure of Chloride Bound Structure of Oxidized BA3-Type Cytochrome C Oxidase Confirmed By Single-Wavelength Anomalous Diffraction, PDB code: 9gdf was solved by A.Kabbinale, J.Johannesson, D.Finke, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 74.54 / 2.28
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 143.688, 98.34, 94.085, 90, 127.58, 90
R / Rfree (%) 15.3 / 19.7

Other elements in 9gdf:

The structure of Chloride Bound Structure of Oxidized BA3-Type Cytochrome C Oxidase Confirmed By Single-Wavelength Anomalous Diffraction also contains other interesting chemical elements:

Copper (Cu) 3 atoms
Chlorine (Cl) 2 atoms

Iron Binding Sites:

The binding sites of Iron atom in the Chloride Bound Structure of Oxidized BA3-Type Cytochrome C Oxidase Confirmed By Single-Wavelength Anomalous Diffraction (pdb code 9gdf). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Chloride Bound Structure of Oxidized BA3-Type Cytochrome C Oxidase Confirmed By Single-Wavelength Anomalous Diffraction, PDB code: 9gdf:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in 9gdf

Go back to Iron Binding Sites List in 9gdf
Iron binding site 1 out of 2 in the Chloride Bound Structure of Oxidized BA3-Type Cytochrome C Oxidase Confirmed By Single-Wavelength Anomalous Diffraction


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Chloride Bound Structure of Oxidized BA3-Type Cytochrome C Oxidase Confirmed By Single-Wavelength Anomalous Diffraction within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe602

b:36.4
occ:1.00
FE A:HEM602 0.0 36.4 1.0
ND A:HEM602 1.9 35.7 1.0
NA A:HEM602 2.0 32.2 1.0
NC A:HEM602 2.0 31.6 1.0
NE2 A:HIS386 2.0 38.8 1.0
NB A:HEM602 2.1 33.6 1.0
NE2 A:HIS72 2.1 36.1 1.0
C1D A:HEM602 2.9 30.6 1.0
C4D A:HEM602 2.9 37.7 1.0
C4B A:HEM602 3.0 35.4 1.0
CE1 A:HIS386 3.0 36.5 1.0
C4C A:HEM602 3.0 32.1 1.0
C1A A:HEM602 3.0 34.4 1.0
C4A A:HEM602 3.0 31.8 1.0
CD2 A:HIS72 3.0 32.1 1.0
C1C A:HEM602 3.1 36.7 1.0
C1B A:HEM602 3.1 31.9 1.0
CD2 A:HIS386 3.1 34.0 1.0
CE1 A:HIS72 3.1 39.9 1.0
CHD A:HEM602 3.3 33.8 1.0
CHA A:HEM602 3.4 35.3 1.0
CHC A:HEM602 3.4 33.4 1.0
CHB A:HEM602 3.5 32.9 1.0
ND1 A:HIS386 4.1 39.6 1.0
CG A:HIS386 4.2 37.4 1.0
C3C A:HEM602 4.2 33.6 1.0
C2D A:HEM602 4.2 38.6 1.0
C3A A:HEM602 4.2 33.2 1.0
C3D A:HEM602 4.2 35.7 1.0
CG A:HIS72 4.2 35.1 1.0
C2A A:HEM602 4.2 34.0 1.0
ND1 A:HIS72 4.2 36.4 1.0
C2C A:HEM602 4.2 32.0 1.0
C3B A:HEM602 4.3 36.7 1.0
C2B A:HEM602 4.3 34.1 1.0
OE1 A:GLN42 4.6 46.8 1.0

Iron binding site 2 out of 2 in 9gdf

Go back to Iron Binding Sites List in 9gdf
Iron binding site 2 out of 2 in the Chloride Bound Structure of Oxidized BA3-Type Cytochrome C Oxidase Confirmed By Single-Wavelength Anomalous Diffraction


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Chloride Bound Structure of Oxidized BA3-Type Cytochrome C Oxidase Confirmed By Single-Wavelength Anomalous Diffraction within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe603

b:37.7
occ:1.00
FE A:HAS603 0.0 37.7 1.0
ND A:HAS603 2.1 33.8 1.0
NA A:HAS603 2.1 32.9 1.0
NE2 A:HIS384 2.1 37.9 1.0
NB A:HAS603 2.1 35.3 1.0
NC A:HAS603 2.1 32.5 1.0
CL A:CL617 2.9 47.0 1.0
C4D A:HAS603 3.0 34.9 1.0
CE1 A:HIS384 3.1 48.5 1.0
C1D A:HAS603 3.1 36.0 1.0
C1A A:HAS603 3.1 29.3 1.0
C4A A:HAS603 3.1 30.6 1.0
C1C A:HAS603 3.1 32.1 1.0
C4C A:HAS603 3.1 33.5 1.0
C4B A:HAS603 3.1 32.6 1.0
C1B A:HAS603 3.1 34.0 1.0
CD2 A:HIS384 3.1 43.8 1.0
CHA A:HAS603 3.4 33.0 1.0
CHB A:HAS603 3.5 35.2 1.0
CHC A:HAS603 3.5 35.0 1.0
CHD A:HAS603 3.5 34.1 1.0
ND1 A:HIS384 4.2 37.5 1.0
CG A:HIS384 4.3 39.0 1.0
C2D A:HAS603 4.3 38.5 1.0
C3D A:HAS603 4.3 34.7 1.0
C3A A:HAS603 4.4 31.6 1.0
C2A A:HAS603 4.4 32.3 1.0
C3C A:HAS603 4.4 36.0 1.0
C2C A:HAS603 4.4 37.5 1.0
C2B A:HAS603 4.5 32.1 1.0
C3B A:HAS603 4.5 32.6 1.0
CU A:CU601 4.8 39.0 1.0
ND2 A:ASN366 4.9 44.2 1.0
CA A:GLY363 5.0 37.2 1.0

Reference:

D.Zoric, J.Johannesson, A.Kabbinale, E.Sandelin, A.Vallejos, S.Ghosh, P.Dahl, J.Ronnholm, M.Bjelcic, A.Finke, C.Bostedt, C.Bacellar Cases Da Silveira, E.Beale, C.Cirelli, P.Johnson, D.Ozerov, S.Boutet, A.Batyuk, C.Kupitz, A.Peck, F.Poitevin, R.Sierra, S.Lisova, C.Wallentin, G.Branden, L.Ostojic, J.Glerup, R.Neutze. Structural Changes in Cytochrome C Oxidase Following the Reduction of Dioxygen to Water To Be Published.
Page generated: Sat Aug 23 03:13:39 2025

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