Iron in PDB 5sxq: Crystal Structure of B. Pseudomallei Katg with Isonicotinic Acid Hydrazide Bound

All present enzymatic activity of Crystal Structure of B. Pseudomallei Katg with Isonicotinic Acid Hydrazide Bound:
1.11.1.21;

The structure of Crystal Structure of B. Pseudomallei Katg with Isonicotinic Acid Hydrazide Bound, PDB code: 5sxq was solved by P.C.Loewen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 2.10
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	100.069, 113.319, 174.640, 90.00, 90.00, 90.00
R / Rfree (%)	15.2 / 18.7

The structure of Crystal Structure of B. Pseudomallei Katg with Isonicotinic Acid Hydrazide Bound also contains other interesting chemical elements:

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

The binding sites of Iron atom in the Crystal Structure of B. Pseudomallei Katg with Isonicotinic Acid Hydrazide Bound (pdb code 5sxq). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Crystal Structure of B. Pseudomallei Katg with Isonicotinic Acid Hydrazide Bound, PDB code: 5sxq:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Crystal Structure of B. Pseudomallei Katg with Isonicotinic Acid Hydrazide Bound


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 B. Pseudomallei Katg with Isonicotinic Acid Hydrazide Bound within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe801 b:23.0 occ:1.00 FE A:HEM801 0.0 23.0 1.0 ND A:HEM801 1.9 23.4 1.0 NE2 A:HIS279 2.0 25.1 1.0 NA A:HEM801 2.1 24.5 1.0 NB A:HEM801 2.1 23.6 1.0 NC A:HEM801 2.1 22.7 1.0 O A:HOH924 2.5 31.6 1.0 C4D A:HEM801 2.9 22.8 1.0 C1D A:HEM801 2.9 22.1 1.0 CD2 A:HIS279 3.0 23.9 1.0 CE1 A:HIS279 3.0 26.9 1.0 C1B A:HEM801 3.0 23.5 1.0 C1A A:HEM801 3.0 24.5 1.0 C4C A:HEM801 3.0 22.1 1.0 C4B A:HEM801 3.1 21.9 1.0 C4A A:HEM801 3.1 23.9 1.0 C1C A:HEM801 3.1 22.1 1.0 CHD A:HEM801 3.3 21.9 1.0 CHA A:HEM801 3.4 24.1 1.0 CHB A:HEM801 3.4 23.8 1.0 CHC A:HEM801 3.4 20.8 1.0 ND1 A:HIS279 4.1 24.8 1.0 CG A:HIS279 4.1 24.0 1.0 C2D A:HEM801 4.2 22.7 1.0 C3D A:HEM801 4.2 22.2 1.0 O1 A:OXY804 4.2 40.4 1.0 C2A A:HEM801 4.2 25.0 1.0 C2B A:HEM801 4.2 23.5 1.0 C3A A:HEM801 4.3 25.1 1.0 NE1 A:TRP111 4.3 20.1 1.0 C3C A:HEM801 4.3 22.6 1.0 C2C A:HEM801 4.3 21.7 1.0 C3B A:HEM801 4.3 22.4 1.0 O1 A:OXY805 4.5 40.8 1.0 O2 A:OXY805 4.5 52.2 1.0 CD1 A:TRP111 4.6 19.2 1.0

Iron binding site 2 out of 2 in the Crystal Structure of B. Pseudomallei Katg with Isonicotinic Acid Hydrazide Bound


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 B. Pseudomallei Katg with Isonicotinic Acid Hydrazide Bound within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe801 b:18.1 occ:1.00 FE B:HEM801 0.0 18.1 1.0 ND B:HEM801 1.9 17.6 1.0 NE2 B:HIS279 2.0 19.7 1.0 NA B:HEM801 2.0 17.6 1.0 NB B:HEM801 2.1 17.4 1.0 NC B:HEM801 2.1 17.1 1.0 O B:HOH1087 2.4 27.8 1.0 C4D B:HEM801 2.9 16.8 1.0 C1D B:HEM801 3.0 16.6 1.0 C1A B:HEM801 3.0 17.9 1.0 CE1 B:HIS279 3.0 18.9 1.0 C4B B:HEM801 3.0 17.8 1.0 CD2 B:HIS279 3.0 19.5 1.0 C1B B:HEM801 3.0 19.0 1.0 C4C B:HEM801 3.0 17.4 1.0 C4A B:HEM801 3.1 19.2 1.0 C1C B:HEM801 3.1 17.3 1.0 CHA B:HEM801 3.3 16.9 1.0 CHC B:HEM801 3.4 16.1 1.0 CHD B:HEM801 3.4 17.2 1.0 CHB B:HEM801 3.5 18.0 1.0 ND1 B:HIS279 4.1 17.5 1.0 C2D B:HEM801 4.1 16.6 1.0 CG B:HIS279 4.1 18.8 1.0 C3D B:HEM801 4.2 17.1 1.0 C2A B:HEM801 4.2 17.5 1.0 C3A B:HEM801 4.2 18.0 1.0 O1 B:OXY805 4.3 37.1 1.0 C2B B:HEM801 4.3 19.4 1.0 C3C B:HEM801 4.3 17.8 1.0 C3B B:HEM801 4.3 18.6 1.0 C2C B:HEM801 4.3 17.1 1.0 O2 B:OXY805 4.3 53.7 1.0 NE1 B:TRP111 4.3 17.1 1.0 O1 B:OXY804 4.4 26.8 1.0 CD1 B:TRP111 4.6 16.8 1.0

B.Wiseman, X.Carpena, M.Feliz, L.J.Donald, M.Pons, I.Fita, P.C.Loewen. Isonicotinic Acid Hydrazide Conversion to Isonicotinyl-Nad By Catalase-Peroxidases. J. Biol. Chem. V. 285 26662 2010.
ISSN: ESSN 1083-351X
PubMed: 20554537
DOI: 10.1074/JBC.M110.139428