Iron in PDB 5al9: Structure of Leishmania Major Peroxidase D211R Mutant (High Res)

All present enzymatic activity of Structure of Leishmania Major Peroxidase D211R Mutant (High Res):
1.11.1.5;

The structure of Structure of Leishmania Major Peroxidase D211R Mutant (High Res), PDB code: 5al9 was solved by G.Chreifi, S.A.Hollingsworth, H.Li, S.Tripathi, A.P.Arce, H.I.Magana-Garcia, T.L.Poulos, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	36.511 / 1.37
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	142.439, 57.860, 36.620, 90.00, 97.59, 90.00
R / Rfree (%)	18.48 / 20.37

The structure of Structure of Leishmania Major Peroxidase D211R Mutant (High Res) also contains other interesting chemical elements:

Potassium	(K)	1 atom
Calcium	(Ca)	1 atom

The binding sites of Iron atom in the Structure of Leishmania Major Peroxidase D211R Mutant (High Res) (pdb code 5al9). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total only one binding site of Iron was determined in the Structure of Leishmania Major Peroxidase D211R Mutant (High Res), PDB code: 5al9:

Iron binding site 1 out of 1 in the Structure of Leishmania Major Peroxidase D211R Mutant (High Res)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Structure of Leishmania Major Peroxidase D211R Mutant (High Res) within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe305 b:8.1 occ:1.00 FE A:HEM305 0.0 8.1 1.0 NA A:HEM305 2.0 6.4 1.0 NC A:HEM305 2.0 6.6 1.0 NB A:HEM305 2.1 8.2 1.0 ND A:HEM305 2.1 6.4 1.0 NE2 A:HIS192 2.1 8.9 1.0 O A:HOH2054 2.2 22.9 1.0 C1A A:HEM305 3.0 8.6 1.0 C4A A:HEM305 3.0 7.4 1.0 C4D A:HEM305 3.1 7.2 1.0 C4B A:HEM305 3.1 8.9 1.0 C1D A:HEM305 3.1 6.7 1.0 C1B A:HEM305 3.1 8.7 1.0 C4C A:HEM305 3.1 5.0 1.0 C1C A:HEM305 3.1 7.5 1.0 CE1 A:HIS192 3.1 11.2 1.0 CD2 A:HIS192 3.1 10.3 1.0 CHB A:HEM305 3.4 8.1 1.0 CHA A:HEM305 3.4 8.0 1.0 CHD A:HEM305 3.4 5.9 1.0 CHC A:HEM305 3.4 9.3 1.0 O A:HOH2055 4.2 24.2 1.0 ND1 A:HIS192 4.2 11.3 1.0 NE1 A:TRP67 4.2 12.9 1.0 CG A:HIS192 4.2 7.8 1.0 C2D A:HEM305 4.2 8.6 1.0 C2B A:HEM305 4.3 8.4 1.0 C2A A:HEM305 4.3 10.3 1.0 C3D A:HEM305 4.3 9.4 1.0 C3B A:HEM305 4.3 9.1 1.0 C3A A:HEM305 4.3 11.1 1.0 C3C A:HEM305 4.3 6.9 1.0 C2C A:HEM305 4.3 8.5 1.0 O A:HOH2049 4.5 36.1 1.0 CD1 A:TRP67 4.7 11.5 1.0 CH2 A:TRP208 5.0 12.2 1.0

G.Chreifi, S.A.Hollingsworth, H.Li, S.Tripathi, A.P.Arce, H.I.Magana-Garcia, T.L.Poulos. Enzymatic Mechanism of Leishmania Major Peroxidase and the Critical Role of Specific Ionic Interactions. Biochemistry 2015.
ISSN: ESSN 1520-4995
PubMed: 25941976
DOI: 10.1021/ACS.BIOCHEM.5B00338