Iron in PDB 4xiy: Crystal Structure of Ketol-Acid Reductoisomerase From Azotobacter

All present enzymatic activity of Crystal Structure of Ketol-Acid Reductoisomerase From Azotobacter:
1.1.1.86;

The structure of Crystal Structure of Ketol-Acid Reductoisomerase From Azotobacter, PDB code: 4xiy was solved by T.Spatzal, J.K.B.Cahn, J.A.Wiig, O.Einsle, Y.Hu, M.W.Ribbe, F.H.Arnold, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	55.79 / 2.50
Space group	P 21 3
Cell size a, b, c (Å), α, β, γ (°)	185.050, 185.050, 185.050, 90.00, 90.00, 90.00
R / Rfree (%)	19.4 / 24.4

The structure of Crystal Structure of Ketol-Acid Reductoisomerase From Azotobacter also contains other interesting chemical elements:

Magnesium

(Mg)

4 atoms

The binding sites of Iron atom in the Crystal Structure of Ketol-Acid Reductoisomerase From Azotobacter (pdb code 4xiy). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 4 binding sites of Iron where determined in the Crystal Structure of Ketol-Acid Reductoisomerase From Azotobacter, PDB code: 4xiy:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in the Crystal Structure of Ketol-Acid Reductoisomerase From Azotobacter


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Crystal Structure of Ketol-Acid Reductoisomerase From Azotobacter within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe402 b:95.0 occ:1.00 OD2 A:ASP190 2.5 37.8 1.0 OE2 A:GLU194 2.6 31.1 1.0 CD A:GLU194 3.3 30.3 1.0 OE1 A:GLU194 3.3 31.8 1.0 CG A:ASP190 3.6 36.1 1.0 OD1 A:ASP190 4.0 44.8 1.0 O A:HOH503 4.0 43.8 1.0 OG B:SER251 4.1 34.4 1.0 CB B:ALA254 4.3 22.8 1.0 NE2 A:HIS107 4.6 47.1 1.0 CG A:GLU194 4.8 29.7 1.0 CE1 A:HIS107 4.8 47.7 1.0 CB A:ASP190 4.9 32.6 1.0 CA B:ALA254 4.9 24.8 1.0 N B:ALA254 5.0 25.1 1.0

Iron binding site 2 out of 4 in the Crystal Structure of Ketol-Acid Reductoisomerase From Azotobacter


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Crystal Structure of Ketol-Acid Reductoisomerase From Azotobacter within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe402 b:56.7 occ:1.00 O B:HOH503 2.2 31.7 1.0 OD2 B:ASP190 2.2 40.1 1.0 OE2 B:GLU194 2.4 31.9 1.0 O B:HOH501 2.5 49.8 1.0 O B:HOH504 2.9 42.0 1.0 O A:HOH502 3.2 39.4 1.0 CD B:GLU194 3.2 30.6 1.0 CG B:ASP190 3.3 36.1 1.0 OE1 B:GLU194 3.3 31.1 1.0 OD1 B:ASP190 3.7 41.4 1.0 OG A:SER251 4.3 34.1 1.0 O B:HOH506 4.4 53.1 1.0 CE1 B:HIS107 4.5 51.7 1.0 CB A:ALA254 4.5 28.1 1.0 NE2 B:HIS107 4.5 52.9 1.0 CB B:ASP190 4.6 31.3 1.0 CG B:GLU194 4.6 30.4 1.0 O B:HOH507 4.7 61.6 1.0 ND1 B:HIS107 4.8 56.1 1.0 MG A:MG401 4.8 54.8 1.0 CD2 B:HIS107 4.9 55.2 1.0 O B:ASP190 4.9 27.2 1.0 N A:ALA254 5.0 27.1 1.0

Iron binding site 3 out of 4 in the Crystal Structure of Ketol-Acid Reductoisomerase From Azotobacter


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Crystal Structure of Ketol-Acid Reductoisomerase From Azotobacter within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe401 b:74.2 occ:1.00 OD2 C:ASP190 2.1 47.4 1.0 OE2 C:GLU194 2.3 32.5 1.0 O C:HOH501 3.0 41.8 1.0 CG C:ASP190 3.0 43.2 1.0 OD1 C:ASP190 3.3 56.4 1.0 CD C:GLU194 3.3 32.5 1.0 OE1 C:GLU194 3.6 36.8 1.0 O D:HOH504 4.4 29.7 1.0 CB C:ASP190 4.4 36.8 1.0 CB D:ALA254 4.4 26.7 1.0 MG D:MG401 4.4 58.5 1.0 NE2 C:HIS107 4.7 52.0 1.0 CE1 C:HIS107 4.7 53.8 1.0 CG C:GLU194 4.7 31.9 1.0 O C:ASP190 4.7 29.1 1.0 OG D:SER251 4.7 32.0 1.0 C C:ASP190 4.9 29.1 1.0

Iron binding site 4 out of 4 in the Crystal Structure of Ketol-Acid Reductoisomerase From Azotobacter


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Crystal Structure of Ketol-Acid Reductoisomerase From Azotobacter within 5.0Å range: probe atom residue distance (Å) B Occ D:Fe402 b:59.8 occ:1.00 O D:HOH502 2.3 34.1 1.0 OE2 D:GLU194 2.3 39.4 1.0 OD2 D:ASP190 2.4 35.0 1.0 O D:HOH508 2.6 48.2 1.0 O C:HOH505 2.7 29.3 1.0 O D:HOH503 2.9 44.2 1.0 CD D:GLU194 3.2 36.9 1.0 CG D:ASP190 3.3 34.6 1.0 OD1 D:ASP190 3.4 45.4 1.0 OE1 D:GLU194 3.5 34.0 1.0 O C:HOH506 4.1 48.4 1.0 O D:HOH509 4.4 55.4 1.0 CB C:ALA254 4.5 25.8 1.0 O D:ASP190 4.5 24.7 1.0 OG C:SER251 4.5 31.9 1.0 MG C:MG402 4.6 54.4 1.0 CG D:GLU194 4.6 35.9 1.0 CB D:ASP190 4.7 28.1 1.0 NE2 D:HIS107 5.0 54.2 1.0

J.K.Cahn, S.Brinkmann-Chen, T.Spatzal, J.A.Wiig, A.R.Buller, O.Einsle, Y.Hu, M.W.Ribbe, F.H.Arnold. Cofactor Specificity Motifs and the Induced Fit Mechanism in Class I Ketol-Acid Reductoisomerases. Biochem.J. 2015.
ISSN: ESSN 1470-8728
PubMed: 25849365
DOI: 10.1042/BJ20150183