Iron in PDB 3hb6: Inactive Mutant H54F of Proteus Mirabilis Catalase

All present enzymatic activity of Inactive Mutant H54F of Proteus Mirabilis Catalase:
1.11.1.6;

The structure of Inactive Mutant H54F of Proteus Mirabilis Catalase, PDB code: 3hb6 was solved by P.Andeoletti, H.M.Jouve, P.Gouet, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	14.97 / 2.30
Space group	P 62 2 2
Cell size a, b, c (Å), α, β, γ (°)	109.300, 109.300, 249.100, 90.00, 90.00, 120.00
R / Rfree (%)	20.3 / 23.6

The binding sites of Iron atom in the Inactive Mutant H54F of Proteus Mirabilis Catalase (pdb code 3hb6). 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 Inactive Mutant H54F of Proteus Mirabilis Catalase, PDB code: 3hb6:

Iron binding site 1 out of 1 in the Inactive Mutant H54F of Proteus Mirabilis Catalase


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Inactive Mutant H54F of Proteus Mirabilis Catalase within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe485 b:24.8 occ:1.00 FE A:HEM485 0.0 24.8 1.0 NB A:HEM485 2.0 21.5 1.0 ND A:HEM485 2.0 20.4 1.0 OH A:TYR337 2.0 25.8 1.0 NA A:HEM485 2.1 20.2 1.0 NC A:HEM485 2.1 22.3 1.0 CZ A:TYR337 2.9 25.7 1.0 C4B A:HEM485 3.0 21.4 1.0 C1B A:HEM485 3.0 21.8 1.0 C4D A:HEM485 3.0 20.6 1.0 C1D A:HEM485 3.0 21.1 1.0 C1C A:HEM485 3.1 22.0 1.0 C1A A:HEM485 3.1 20.6 1.0 C4A A:HEM485 3.1 19.0 1.0 C4C A:HEM485 3.1 22.5 1.0 CHC A:HEM485 3.3 23.1 1.0 CHA A:HEM485 3.4 20.2 1.0 CHB A:HEM485 3.4 21.5 1.0 CHD A:HEM485 3.4 21.7 1.0 CE1 A:TYR337 3.7 25.7 1.0 CE2 A:TYR337 3.7 24.1 1.0 NH2 A:ARG333 4.1 20.2 1.0 NE A:ARG333 4.1 21.8 1.0 CE2 A:PHE54 4.1 26.2 1.0 C3B A:HEM485 4.2 20.9 1.0 C2B A:HEM485 4.2 21.0 1.0 C3D A:HEM485 4.2 19.7 1.0 C2D A:HEM485 4.3 21.4 1.0 C2C A:HEM485 4.3 21.5 1.0 C3C A:HEM485 4.3 20.8 1.0 C2A A:HEM485 4.3 19.9 1.0 C3A A:HEM485 4.3 21.1 1.0 CZ A:PHE140 4.5 25.1 1.0 CZ A:ARG333 4.5 21.8 1.0 CD2 A:PHE54 4.7 25.4 1.0 CZ A:PHE54 4.9 26.1 1.0 CD1 A:TYR337 4.9 23.1 1.0 CD2 A:TYR337 4.9 23.7 1.0

P.Andreoletti, J.M.Mouesca, P.Gouet, M.Jaquinod, C.Capeillere-Blandin, H.M.Jouve. Verdoheme Formation in Proteus Mirabilis Catalase. Biochim.Biophys.Acta V.1790 741 2009.
ISSN: ISSN 0006-3002
PubMed: 19394409
DOI: 10.1016/J.BBAGEN.2009.04.010