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

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

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:

Chlorine	(Cl)	2 atoms
Sodium	(Na)	4 atoms

The binding sites of Calcium 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 Calcium atom.
In total 4 binding sites of Calcium 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 Calcium binding site number: 1; 2; 3; 4;

Calcium binding site 1 out of 4 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 Calcium with other atoms in the Ca 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:Ca200 b:16.0 occ:1.00 O A:HOH407 2.2 23.2 0.8 O A:TYR59 2.3 15.1 1.0 O A:HOH406 2.3 12.0 1.0 O B:HOH1001 2.4 16.8 1.0 OD2 B:ASP67 2.4 17.6 1.0 OE2 A:GLU61 2.5 23.5 1.0 CG B:ASP67 3.5 16.3 1.0 C A:TYR59 3.5 14.8 1.0 CD A:GLU61 3.7 21.9 1.0 CB B:ASP67 3.9 12.2 1.0 NA A:NA400 4.0 10.5 1.0 O B:HOH1036 4.1 16.7 1.0 O A:TYR58 4.2 18.1 1.0 CB A:TYR59 4.2 13.4 1.0 O B:HOH1129 4.2 16.5 0.6 CG A:GLU61 4.3 18.7 1.0 N A:GLY60 4.4 14.3 1.0 CA A:GLY60 4.4 14.0 1.0 CA A:TYR59 4.5 13.8 1.0 OD1 B:ASP68 4.5 19.6 1.0 O A:HOH547 4.5 40.8 1.0 C A:GLY60 4.5 14.2 1.0 OD1 B:ASP67 4.5 19.0 1.0 CE1 A:TYR97 4.6 14.4 1.0 OE1 A:GLU61 4.6 21.5 1.0 N A:GLU61 4.7 13.2 1.0 O B:CYS64 4.8 15.7 1.0 CD1 A:TYR97 4.9 14.8 1.0 O A:GLY60 5.0 13.1 1.0

Calcium binding site 2 out of 4 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 Calcium with other atoms in the Ca 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 A:Ca350 b:17.1 occ:1.00 O A:HOH409 2.2 13.7 0.9 O4 A:BTB351 2.4 17.4 1.0 O3 A:BTB351 2.4 16.5 1.0 O6 A:BTB351 2.4 17.9 1.0 O A:HOH411 2.4 16.5 1.0 O8 A:BTB351 2.4 17.7 1.0 O A:HOH410 2.4 18.6 0.9 N A:BTB351 2.7 17.3 1.0 C2 A:BTB351 3.3 15.8 1.0 C6 A:BTB351 3.3 16.7 1.0 C3 A:BTB351 3.4 13.8 1.0 C4 A:BTB351 3.4 15.1 1.0 C8 A:BTB351 3.4 15.4 1.0 C5 A:BTB351 3.5 15.8 1.0 C7 A:BTB351 3.6 15.0 1.0 O A:PRO150 4.4 16.5 1.0 OE2 A:GLU146 4.5 16.0 1.0 OE1 A:GLU146 4.6 17.3 1.0 O A:HOH448 4.7 13.5 1.0 O A:HOH535 4.7 25.2 1.0 C1 A:BTB351 4.8 17.1 1.0 CD A:GLU146 4.9 13.7 1.0 O A:HOH417 5.0 19.8 1.0

Calcium binding site 3 out of 4 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 Calcium with other atoms in the Ca binding site number 3 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:Ca1000 b:21.1 occ:1.00 O A:HOH408 2.3 17.9 1.0 O B:TYR59 2.3 16.0 1.0 O B:HOH1003 2.3 26.6 0.7 O B:HOH1002 2.3 14.2 1.0 OD2 A:ASP67 2.5 24.0 1.0 OE2 B:GLU61 2.7 21.9 1.0 C B:TYR59 3.5 16.8 1.0 CG A:ASP67 3.6 21.9 1.0 CD B:GLU61 3.8 20.3 1.0 O B:TYR58 4.0 16.6 1.0 CB B:TYR59 4.1 17.3 1.0 NA A:NA401 4.2 13.3 1.0 CB A:ASP67 4.2 20.2 1.0 O A:HOH470 4.2 10.6 1.0 CG B:GLU61 4.3 18.4 1.0 OD1 A:ASP68 4.3 30.5 1.0 N B:GLY60 4.4 17.0 1.0 CA B:TYR59 4.4 17.7 1.0 O A:HOH484 4.4 25.4 0.5 CA B:GLY60 4.5 15.5 1.0 CE1 B:TYR97 4.6 25.4 1.0 C B:GLY60 4.6 15.9 1.0 OD1 A:ASP67 4.6 21.3 1.0 O B:HOH1046 4.8 28.4 1.0 OE1 B:GLU61 4.8 18.6 1.0 N B:GLU61 4.9 16.3 1.0 O A:CYS64 4.9 22.3 1.0 O B:HOH1074 5.0 30.3 1.0

Calcium binding site 4 out of 4 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 Calcium with other atoms in the Ca binding site number 4 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:Ca300 b:31.1 occ:1.00 O6 B:BTB301 2.2 37.1 1.0 O B:HOH1005 2.3 25.2 0.8 O B:HOH1004 2.3 26.6 1.0 O4 B:BTB301 2.4 33.6 1.0 O8 B:BTB301 2.5 36.4 1.0 O3 B:BTB301 2.5 28.8 1.0 N B:BTB301 2.6 37.4 1.0 C6 B:BTB301 3.2 37.5 1.0 C2 B:BTB301 3.3 35.6 1.0 C4 B:BTB301 3.4 32.3 1.0 C3 B:BTB301 3.4 33.8 1.0 C5 B:BTB301 3.4 37.4 1.0 C8 B:BTB301 3.5 36.3 1.0 C7 B:BTB301 3.5 36.1 1.0 O B:ARG148 3.9 24.8 1.0 O B:HOH1150 4.2 35.1 1.0 OE1 B:GLU151 4.2 34.3 1.0 O B:HOH1011 4.3 26.0 1.0 OE2 B:GLU151 4.3 31.1 1.0 CD B:GLU151 4.6 32.8 1.0 C1 B:BTB301 4.8 35.8 1.0

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