Iron in PDB 5kzl: Structure of Heme Oxygenase From Leptospira Interrogans

All present enzymatic activity of Structure of Heme Oxygenase From Leptospira Interrogans:
1.14.14.18;

The structure of Structure of Heme Oxygenase From Leptospira Interrogans, PDB code: 5kzl was solved by S.Klinke, A.Soldano, L.H.Otero, M.Rivera, D.L.Catalano-Dupuy, E.A.Ceccarelli, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	31.70 / 1.73
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	37.640, 58.790, 86.700, 90.00, 90.00, 90.00
R / Rfree (%)	18.4 / 22.2

The binding sites of Iron atom in the Structure of Heme Oxygenase From Leptospira Interrogans (pdb code 5kzl). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Structure of Heme Oxygenase From Leptospira Interrogans, PDB code: 5kzl:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Structure of Heme Oxygenase From Leptospira Interrogans


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Structure of Heme Oxygenase From Leptospira Interrogans within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe301 b:6.9 occ:0.50 FE A:HEM301 0.0 6.9 0.5 FE A:HEM301 0.0 16.8 0.5 ND A:HEM301 1.9 7.0 0.5 ND A:HEM301 2.0 16.8 0.5 NA A:HEM301 2.0 17.0 0.5 NA A:HEM301 2.0 7.1 0.5 NC A:HEM301 2.1 16.7 0.5 NB A:HEM301 2.1 6.6 0.5 NB A:HEM301 2.1 16.5 0.5 NC A:HEM301 2.1 6.9 0.5 O A:HOH467 2.3 13.6 1.0 NE2 A:HIS15 2.3 20.1 1.0 C1D A:HEM301 2.9 7.4 0.5 C4D A:HEM301 2.9 17.1 0.5 C4C A:HEM301 2.9 16.9 0.5 C1D A:HEM301 2.9 17.2 0.5 C4D A:HEM301 2.9 7.3 0.5 C4B A:HEM301 2.9 6.9 0.5 C1A A:HEM301 3.0 7.2 0.5 C4A A:HEM301 3.0 17.0 0.5 C4B A:HEM301 3.0 16.8 0.5 C1A A:HEM301 3.0 17.1 0.5 C1B A:HEM301 3.0 7.0 0.5 C1B A:HEM301 3.0 16.9 0.5 C4C A:HEM301 3.0 7.1 0.5 C4A A:HEM301 3.0 7.0 0.5 C1C A:HEM301 3.0 6.8 0.5 C1C A:HEM301 3.1 16.6 0.5 CE1 A:HIS15 3.2 20.1 1.0 CD2 A:HIS15 3.3 20.5 1.0 CHD A:HEM301 3.3 17.6 0.5 CHD A:HEM301 3.3 7.8 0.5 CHC A:HEM301 3.3 7.5 0.5 CHB A:HEM301 3.3 17.3 0.5 CHA A:HEM301 3.4 7.7 0.5 CHC A:HEM301 3.4 17.3 0.5 CHA A:HEM301 3.4 17.6 0.5 CHB A:HEM301 3.4 7.4 0.5 C3C A:HEM301 4.2 17.2 0.5 O A:HOH573 4.2 10.8 1.0 C3A A:HEM301 4.2 17.5 0.5 C2A A:HEM301 4.2 17.6 0.5 C2D A:HEM301 4.2 7.8 0.5 C2D A:HEM301 4.2 17.5 0.5 C3D A:HEM301 4.2 7.9 0.5 C3A A:HEM301 4.2 7.6 0.5 C3B A:HEM301 4.2 7.3 0.5 C2A A:HEM301 4.2 7.7 0.5 C3D A:HEM301 4.2 17.6 0.5 C3C A:HEM301 4.2 7.5 0.5 C2B A:HEM301 4.3 7.1 0.5 C2C A:HEM301 4.3 17.2 0.5 C2B A:HEM301 4.3 17.0 0.5 C2C A:HEM301 4.3 7.4 0.5 C3B A:HEM301 4.3 17.2 0.5 ND1 A:HIS15 4.4 21.1 1.0 CG A:HIS15 4.4 19.9 1.0 CA A:GLY128 4.7 5.2 1.0 O A:GLY128 4.7 6.7 1.0

Iron binding site 2 out of 2 in the Structure of Heme Oxygenase From Leptospira Interrogans


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Structure of Heme Oxygenase From Leptospira Interrogans within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe301 b:16.8 occ:0.50 FE A:HEM301 0.0 16.8 0.5 FE A:HEM301 0.0 6.9 0.5 ND A:HEM301 2.0 7.0 0.5 ND A:HEM301 2.0 16.8 0.5 NA A:HEM301 2.0 17.0 0.5 NA A:HEM301 2.0 7.1 0.5 NC A:HEM301 2.1 16.7 0.5 NB A:HEM301 2.1 6.6 0.5 NB A:HEM301 2.1 16.5 0.5 NC A:HEM301 2.1 6.9 0.5 NE2 A:HIS15 2.3 20.1 1.0 O A:HOH467 2.3 13.6 1.0 C4C A:HEM301 2.9 16.9 0.5 C1D A:HEM301 2.9 17.2 0.5 C4D A:HEM301 2.9 17.1 0.5 C4B A:HEM301 2.9 6.9 0.5 C1D A:HEM301 2.9 7.4 0.5 C4D A:HEM301 2.9 7.3 0.5 C1A A:HEM301 3.0 7.2 0.5 C1B A:HEM301 3.0 7.0 0.5 C4B A:HEM301 3.0 16.8 0.5 C4A A:HEM301 3.0 17.0 0.5 C1A A:HEM301 3.0 17.1 0.5 C4A A:HEM301 3.0 7.0 0.5 C1B A:HEM301 3.0 16.9 0.5 C4C A:HEM301 3.0 7.1 0.5 C1C A:HEM301 3.0 6.8 0.5 C1C A:HEM301 3.0 16.6 0.5 CE1 A:HIS15 3.2 20.1 1.0 CD2 A:HIS15 3.3 20.5 1.0 CHD A:HEM301 3.3 17.6 0.5 CHC A:HEM301 3.3 7.5 0.5 CHD A:HEM301 3.3 7.8 0.5 CHA A:HEM301 3.4 7.7 0.5 CHB A:HEM301 3.4 17.3 0.5 CHC A:HEM301 3.4 17.3 0.5 CHA A:HEM301 3.4 17.6 0.5 CHB A:HEM301 3.4 7.4 0.5 C3C A:HEM301 4.1 17.2 0.5 O A:HOH573 4.2 10.8 1.0 C2D A:HEM301 4.2 17.5 0.5 C3A A:HEM301 4.2 7.6 0.5 C3B A:HEM301 4.2 7.3 0.5 C2A A:HEM301 4.2 7.7 0.5 C3A A:HEM301 4.2 17.5 0.5 C2A A:HEM301 4.2 17.6 0.5 C3D A:HEM301 4.2 7.9 0.5 C3D A:HEM301 4.2 17.6 0.5 C2D A:HEM301 4.2 7.8 0.5 C2B A:HEM301 4.2 7.1 0.5 C2C A:HEM301 4.2 17.2 0.5 C3C A:HEM301 4.2 7.5 0.5 C2B A:HEM301 4.3 17.0 0.5 C2C A:HEM301 4.3 7.4 0.5 C3B A:HEM301 4.3 17.2 0.5 ND1 A:HIS15 4.4 21.1 1.0 CG A:HIS15 4.4 19.9 1.0 CA A:GLY128 4.7 5.2 1.0 O A:GLY128 4.7 6.7 1.0

A.Soldano, S.Klinke, L.H.Otero, M.Rivera, D.L.Catalano-Dupuy, E.A.Ceccarelli. Structural and Mutational Analyses of the Leptospira Interrogans Virulence-Related Heme Oxygenase Provide Insights Into Its Catalytic Mechanism. Plos One V. 12 82535 2017.
ISSN: ESSN 1932-6203
PubMed: 28771589
DOI: 10.1371/JOURNAL.PONE.0182535