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Chlorine in PDB 1ag9: Flavodoxins That Are Required For Enzyme Activation: the Structure of Oxidized Flavodoxin From Escherichia Coli at 1.8 Angstroms Resolution.

Protein crystallography data

The structure of Flavodoxins That Are Required For Enzyme Activation: the Structure of Oxidized Flavodoxin From Escherichia Coli at 1.8 Angstroms Resolution., PDB code: 1ag9 was solved by D.M.Hoover, M.L.Ludwig, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 10.00 / 1.80
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 126.400, 41.100, 68.150, 90.00, 90.00, 90.00
R / Rfree (%) 19.6 / 25

Other elements in 1ag9:

The structure of Flavodoxins That Are Required For Enzyme Activation: the Structure of Oxidized Flavodoxin From Escherichia Coli at 1.8 Angstroms Resolution. also contains other interesting chemical elements:

Calcium (Ca) 4 atoms
Sodium (Na) 4 atoms

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Flavodoxins That Are Required For Enzyme Activation: the Structure of Oxidized Flavodoxin From Escherichia Coli at 1.8 Angstroms Resolution. (pdb code 1ag9). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Flavodoxins That Are Required For Enzyme Activation: the Structure of Oxidized Flavodoxin From Escherichia Coli at 1.8 Angstroms Resolution., PDB code: 1ag9:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in 1ag9

Go back to Chlorine Binding Sites List in 1ag9
Chlorine binding site 1 out of 2 in the Flavodoxins That Are Required For Enzyme Activation: the Structure of Oxidized Flavodoxin From Escherichia Coli at 1.8 Angstroms Resolution.


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Flavodoxins That Are Required For Enzyme Activation: the Structure of Oxidized Flavodoxin From Escherichia Coli at 1.8 Angstroms Resolution. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl405

b:20.4
occ:1.00
O A:HOH538 2.8 32.2 0.4
O A:HOH512 2.9 32.7 1.0
O A:HOH422 3.0 12.6 0.8
O B:HOH1052 3.2 19.4 1.0
N A:ALA62 3.3 14.3 1.0
CB A:ALA62 3.7 14.0 1.0
OE1 A:GLU61 3.8 21.5 1.0
CG2 A:THR104 3.8 12.2 1.0
CA A:GLU61 4.0 14.2 1.0
CA A:ALA62 4.1 14.3 1.0
C A:GLU61 4.1 14.2 1.0
OD1 A:ASP67 4.3 21.3 1.0
CE2 A:PHE70 4.4 19.4 1.0
O B:HOH1151 4.4 33.3 0.9
OG1 A:THR104 4.4 13.4 1.0
O A:GLY60 4.4 13.1 1.0
CD A:GLU61 4.5 21.9 1.0
CB A:THR104 4.6 11.6 1.0
CB A:GLU61 4.6 15.3 1.0
O B:HOH1116 4.8 31.3 1.0
NA A:NA400 4.9 10.5 1.0
O A:HOH470 4.9 10.6 1.0
NA A:NA401 4.9 13.3 1.0

Chlorine binding site 2 out of 2 in 1ag9

Go back to Chlorine Binding Sites List in 1ag9
Chlorine binding site 2 out of 2 in the Flavodoxins That Are Required For Enzyme Activation: the Structure of Oxidized Flavodoxin From Escherichia Coli at 1.8 Angstroms Resolution.


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Flavodoxins That Are Required For Enzyme Activation: the Structure of Oxidized Flavodoxin From Escherichia Coli at 1.8 Angstroms Resolution. within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl404

b:22.7
occ:1.00
O B:HOH1073 2.7 30.3 0.8
O A:HOH474 3.0 15.4 0.6
O B:HOH1053 3.0 17.6 1.0
O B:HOH1074 3.2 30.3 1.0
N B:ALA62 3.3 15.3 1.0
CB B:ALA62 3.7 10.7 1.0
CG2 B:THR104 3.8 19.6 1.0
OE1 B:GLU61 3.8 18.6 1.0
CA B:GLU61 4.0 16.5 1.0
CA B:ALA62 4.1 13.7 1.0
C B:GLU61 4.1 16.9 1.0
O B:HOH1116 4.2 31.3 1.0
OD1 B:ASP67 4.3 19.0 1.0
O B:GLY60 4.4 14.4 1.0
CE2 B:PHE70 4.4 15.8 1.0
OG1 B:THR104 4.4 20.0 1.0
CD B:GLU61 4.5 20.3 1.0
CB B:THR104 4.6 20.8 1.0
CB B:GLU61 4.6 16.9 1.0
O B:HOH1036 4.9 16.7 1.0
O B:HOH1151 4.9 33.3 0.9
NA A:NA400 4.9 10.5 1.0
NA A:NA401 5.0 13.3 1.0
OE2 B:GLU61 5.0 21.9 1.0

Reference:

D.M.Hoover, M.L.Ludwig. A Flavodoxin That Is Required For Enzyme Activation: the Structure of Oxidized Flavodoxin From Escherichia Coli at 1.8 A Resolution. Protein Sci. V. 6 2525 1997.
ISSN: ISSN 0961-8368
PubMed: 9416602
Page generated: Thu Jul 10 16:16:34 2025

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