Iron in PDB 5sx3: Crystal Structure of the Catalase-Peroxidase Katg of B. Pseudomaallei at pH 4.5

All present enzymatic activity of Crystal Structure of the Catalase-Peroxidase Katg of B. Pseudomaallei at pH 4.5:
1.11.1.21;

The structure of Crystal Structure of the Catalase-Peroxidase Katg of B. Pseudomaallei at pH 4.5, PDB code: 5sx3 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 / 2.00
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	101.049, 114.847, 174.704, 90.00, 90.00, 90.00
R / Rfree (%)	16.2 / 19.6

The structure of Crystal Structure of the Catalase-Peroxidase Katg of B. Pseudomaallei at pH 4.5 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 the Catalase-Peroxidase Katg of B. Pseudomaallei at pH 4.5 (pdb code 5sx3). 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 the Catalase-Peroxidase Katg of B. Pseudomaallei at pH 4.5, PDB code: 5sx3:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Crystal Structure of the Catalase-Peroxidase Katg of B. Pseudomaallei at pH 4.5


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 the Catalase-Peroxidase Katg of B. Pseudomaallei at pH 4.5 within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe801 b:28.3 occ:1.00 FE A:HEM801 0.0 28.3 1.0 ND A:HEM801 2.0 30.2 1.0 NE2 A:HIS279 2.0 31.6 1.0 NB A:HEM801 2.1 29.8 1.0 NA A:HEM801 2.1 31.4 1.0 NC A:HEM801 2.1 27.8 1.0 O A:HOH1197 2.6 46.0 1.0 C1D A:HEM801 3.0 27.7 1.0 C1B A:HEM801 3.0 32.0 1.0 CE1 A:HIS279 3.0 29.3 1.0 C4D A:HEM801 3.0 30.2 1.0 C4A A:HEM801 3.0 31.6 1.0 CD2 A:HIS279 3.0 30.2 1.0 C4B A:HEM801 3.1 28.9 1.0 C1A A:HEM801 3.1 30.6 1.0 C4C A:HEM801 3.1 26.6 1.0 C1C A:HEM801 3.1 27.4 1.0 CHB A:HEM801 3.3 31.4 1.0 CHD A:HEM801 3.4 27.1 1.0 CHA A:HEM801 3.4 30.2 1.0 CHC A:HEM801 3.5 28.5 1.0 ND1 A:HIS279 4.1 29.4 1.0 CG A:HIS279 4.2 28.7 1.0 C2D A:HEM801 4.2 27.8 1.0 C2B A:HEM801 4.2 31.9 1.0 C2A A:HEM801 4.3 32.4 1.0 C3A A:HEM801 4.3 31.8 1.0 C3D A:HEM801 4.3 29.1 1.0 C3B A:HEM801 4.3 30.6 1.0 NE1 A:TRP111 4.3 30.3 1.0 C2C A:HEM801 4.3 27.4 1.0 C3C A:HEM801 4.4 27.8 1.0 O1 A:OXY804 4.5 53.5 1.0 O A:HOH1382 4.5 54.7 1.0 CD1 A:TRP111 4.6 29.4 1.0 O A:HOH936 4.9 57.9 1.0

Iron binding site 2 out of 2 in the Crystal Structure of the Catalase-Peroxidase Katg of B. Pseudomaallei at pH 4.5


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 the Catalase-Peroxidase Katg of B. Pseudomaallei at pH 4.5 within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe801 b:23.8 occ:1.00 FE B:HEM801 0.0 23.8 1.0 ND B:HEM801 2.0 22.6 1.0 NA B:HEM801 2.0 22.8 1.0 NB B:HEM801 2.0 22.6 1.0 NE2 B:HIS279 2.0 27.4 1.0 NC B:HEM801 2.1 21.8 1.0 O B:HOH1251 2.6 32.4 1.0 C4B B:HEM801 2.9 23.4 1.0 C4D B:HEM801 3.0 22.3 1.0 C1A B:HEM801 3.0 22.4 1.0 C1D B:HEM801 3.0 21.6 1.0 C4A B:HEM801 3.0 24.1 1.0 CE1 B:HIS279 3.0 27.1 1.0 C1B B:HEM801 3.0 24.6 1.0 C1C B:HEM801 3.1 22.9 1.0 C4C B:HEM801 3.1 22.3 1.0 CD2 B:HIS279 3.1 26.8 1.0 CHA B:HEM801 3.4 22.2 1.0 CHC B:HEM801 3.4 23.0 1.0 CHB B:HEM801 3.5 23.9 1.0 CHD B:HEM801 3.5 21.7 1.0 ND1 B:HIS279 4.2 26.7 1.0 C2D B:HEM801 4.2 21.9 1.0 C3A B:HEM801 4.2 24.6 1.0 C2A B:HEM801 4.2 23.4 1.0 C3B B:HEM801 4.2 23.6 1.0 CG B:HIS279 4.2 27.1 1.0 C3D B:HEM801 4.2 22.8 1.0 C2B B:HEM801 4.2 23.2 1.0 O B:HOH1378 4.3 44.8 1.0 C2C B:HEM801 4.3 22.9 1.0 C3C B:HEM801 4.3 23.2 1.0 NE1 B:TRP111 4.4 26.6 1.0 O1 B:OXY804 4.5 36.8 1.0 CD1 B:TRP111 4.6 26.4 1.0

X.Carpena, B.Wiseman, T.Deemagarn, B.Herguedas, A.Ivancich, R.Singh, P.C.Loewen, I.Fita. Roles For ARG426 and TRP111 in the Modulation of Nadh Oxidase Activity of the Catalase-Peroxidase Katg From Burkholderia Pseudomallei Inferred From pH-Induced Structural Changes. Biochemistry V. 45 5171 2006.
ISSN: ISSN 0006-2960
PubMed: 16618106