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Chlorine 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
Iron (Fe) 2 atoms

Chlorine Binding Sites:

The binding sites of Chlorine 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 Chlorine atom.
In total 2 binding sites of Chlorine 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 Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in 9gdf

Go back to Chlorine Binding Sites List in 9gdf
Chlorine 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 Chlorine with other atoms in the Cl 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:Cl616

b:48.1
occ:1.00
O11 A:HAS603 2.8 39.6 1.0
OG A:SER309 3.0 46.0 1.0
C12 A:HAS603 3.3 38.2 1.0
C13 A:HAS603 3.5 37.4 1.0
CD2 A:LEU240 3.6 31.7 1.0
CMC A:HAS603 3.6 41.2 1.0
C11 A:HAS603 3.6 37.0 1.0
CZ A:PHE356 3.7 39.5 1.0
CE1 A:TYR237 3.7 37.0 1.0
CB A:SER309 3.7 39.2 1.0
CE2 A:PHE356 3.9 35.2 1.0
C14 A:HAS603 3.9 43.0 1.0
CHC A:HAS603 4.1 35.0 1.0
CD1 A:TYR237 4.4 33.9 1.0
OH A:TYR244 4.5 42.3 1.0
CZ A:TYR237 4.6 36.0 1.0
C3B A:HAS603 4.6 32.6 1.0
OH A:TYR237 4.6 36.3 1.0
C2C A:HAS603 4.7 37.5 1.0
CZ A:PHE272 4.8 38.1 1.0
CE1 A:PHE272 4.8 40.2 1.0
NE2 A:GLN388 4.9 42.7 1.0
C4B A:HAS603 4.9 32.6 1.0
C1C A:HAS603 4.9 32.1 1.0
CE1 A:PHE356 4.9 41.4 1.0
CG A:LEU240 5.0 31.5 1.0

Chlorine binding site 2 out of 2 in 9gdf

Go back to Chlorine Binding Sites List in 9gdf
Chlorine 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 Chlorine with other atoms in the Cl 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:Cl617

b:47.0
occ:1.00
CU A:CU601 2.2 39.0 1.0
FE A:HAS603 2.9 37.7 1.0
ND A:HAS603 3.0 33.8 1.0
NA A:HAS603 3.0 32.9 1.0
ND1 A:HIS233 3.2 34.2 1.0
CE1 A:HIS233 3.4 39.1 1.0
C4D A:HAS603 3.4 34.9 1.0
NE2 A:HIS283 3.5 35.7 1.0
C1A A:HAS603 3.5 29.3 1.0
CE1 A:HIS283 3.6 42.2 1.0
C1D A:HAS603 3.6 36.0 1.0
NC A:HAS603 3.6 32.5 1.0
C4A A:HAS603 3.6 30.6 1.0
NB A:HAS603 3.7 35.3 1.0
CHA A:HAS603 3.7 33.0 1.0
NE2 A:HIS282 3.9 40.6 1.0
CG2 A:VAL236 3.9 34.5 1.0
CG1 A:VAL236 4.1 34.2 1.0
C4C A:HAS603 4.1 33.5 1.0
CHD A:HAS603 4.1 34.1 1.0
CHB A:HAS603 4.2 35.2 1.0
C1B A:HAS603 4.2 34.0 1.0
C3D A:HAS603 4.3 34.7 1.0
C2A A:HAS603 4.4 32.3 1.0
CG A:HIS233 4.4 33.3 1.0
C2D A:HAS603 4.4 38.5 1.0
C1C A:HAS603 4.5 32.1 1.0
C3A A:HAS603 4.5 31.6 1.0
CB A:VAL236 4.6 35.9 1.0
C4B A:HAS603 4.6 32.6 1.0
NE2 A:HIS233 4.6 37.6 1.0
CE1 A:HIS282 4.7 43.5 1.0
CD2 A:HIS283 4.8 37.9 1.0
CD2 A:HIS282 4.8 41.0 1.0
ND1 A:HIS283 4.8 35.8 1.0
CA A:HIS233 4.9 34.1 1.0
NE2 A:HIS384 4.9 37.9 1.0
O A:HIS233 4.9 37.1 1.0
CHC A:HAS603 5.0 35.0 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 00:41:24 2025

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