Iron in PDB 3bxd: Crystal Structure of Mouse Myo-Inositol Oxygenase (Re-Refined)

All present enzymatic activity of Crystal Structure of Mouse Myo-Inositol Oxygenase (Re-Refined):
1.13.99.1;

The structure of Crystal Structure of Mouse Myo-Inositol Oxygenase (Re-Refined), PDB code: 3bxd was solved by B.M.Hallberg, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	42.70 / 2.00
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	44.600, 77.200, 85.400, 90.00, 90.00, 90.00
R / Rfree (%)	21 / 25.5

The binding sites of Iron atom in the Crystal Structure of Mouse Myo-Inositol Oxygenase (Re-Refined) (pdb code 3bxd). 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 Mouse Myo-Inositol Oxygenase (Re-Refined), PDB code: 3bxd:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Crystal Structure of Mouse Myo-Inositol Oxygenase (Re-Refined)


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 Mouse Myo-Inositol Oxygenase (Re-Refined) within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe301 b:44.8 occ:1.00 NE2 A:HIS123 2.1 41.0 1.0 O A:OH304 2.2 52.0 1.0 OD2 A:ASP124 2.3 46.1 1.0 O A:HOH310 2.3 46.4 1.0 NE2 A:HIS98 2.4 55.4 1.0 OD1 A:ASP253 2.4 55.7 1.0 CD2 A:HIS123 3.0 34.4 1.0 CG A:ASP124 3.1 48.4 1.0 HD2 A:HIS123 3.1 27.2 1.0 CE1 A:HIS98 3.2 59.2 1.0 CE1 A:HIS123 3.2 41.7 1.0 HE1 A:HIS98 3.2 50.8 1.0 CG A:ASP253 3.3 55.2 1.0 OD1 A:ASP124 3.3 47.8 1.0 CD2 A:HIS98 3.4 60.7 1.0 HE1 A:HIS123 3.5 33.4 1.0 FE A:FE302 3.5 42.7 1.0 OD2 A:ASP253 3.6 58.0 1.0 HD2 A:HIS98 3.6 52.5 1.0 O1 A:INS303 3.6 38.5 1.0 HZ1 A:LYS127 3.7 59.8 1.0 C1 A:INS303 4.1 51.6 1.0 CG A:HIS123 4.2 42.0 1.0 HB2 A:ASP124 4.3 34.1 1.0 ND1 A:HIS123 4.3 40.6 1.0 ND1 A:HIS98 4.3 56.9 1.0 CB A:ASP124 4.3 40.9 1.0 CG A:HIS98 4.4 64.0 1.0 HE3 A:LYS257 4.4 74.6 1.0 HZ1 A:LYS257 4.5 85.5 1.0 HZ2 A:LYS127 4.5 59.8 1.0 HD2 A:HIS220 4.5 28.0 1.0 NZ A:LYS127 4.5 64.0 1.0 HE2 A:LYS257 4.6 74.6 1.0 HD21 A:ASN95 4.6 51.9 1.0 CB A:ASP253 4.7 57.2 1.0 NE2 A:HIS220 4.7 33.8 1.0 HA A:ASP253 4.7 51.3 1.0 O6 A:INS303 4.7 50.0 1.0 O A:HOH375 4.8 60.2 1.0 O A:ASP253 4.8 58.4 1.0 HZ A:PHE249 4.8 40.9 1.0 HB3 A:ASP124 4.8 34.1 1.0 CD2 A:HIS220 4.8 35.9 1.0 CE A:LYS257 4.9 81.1 1.0 HB2 A:ASP253 4.9 45.3 1.0 OG1 A:THR102 5.0 45.3 1.0

Iron binding site 2 out of 2 in the Crystal Structure of Mouse Myo-Inositol Oxygenase (Re-Refined)


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 Mouse Myo-Inositol Oxygenase (Re-Refined) within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe302 b:42.7 occ:1.00 O1 A:INS303 2.1 38.5 1.0 NE2 A:HIS220 2.1 33.8 1.0 OD1 A:ASP124 2.2 47.8 1.0 O6 A:INS303 2.2 50.0 1.0 O A:OH304 2.4 52.0 1.0 NE2 A:HIS194 2.4 43.5 1.0 C1 A:INS303 2.8 51.6 1.0 C6 A:INS303 2.9 44.0 1.0 CD2 A:HIS220 3.0 35.9 1.0 HD2 A:HIS220 3.1 28.0 1.0 HD2 A:HIS123 3.1 27.2 1.0 CG A:ASP124 3.1 48.4 1.0 CE1 A:HIS220 3.2 44.0 1.0 CD2 A:HIS194 3.2 40.1 1.0 HD2 A:HIS194 3.3 36.3 1.0 HZ1 A:LYS127 3.4 59.8 1.0 OD2 A:ASP124 3.4 46.1 1.0 HE1 A:HIS220 3.4 35.1 1.0 HE3 A:LYS127 3.4 44.5 1.0 CE1 A:HIS194 3.5 45.2 1.0 FE A:FE301 3.5 44.8 1.0 HE1 A:HIS194 3.7 38.4 1.0 OG A:SER221 3.8 46.8 1.0 HG A:SER221 3.9 37.5 1.0 CD2 A:HIS123 3.9 34.4 1.0 CE A:LYS127 4.1 50.6 1.0 NZ A:LYS127 4.2 64.0 1.0 HA A:ASP124 4.2 30.6 1.0 CG A:HIS220 4.2 41.7 1.0 C2 A:INS303 4.2 60.1 1.0 O A:HOH310 4.2 46.4 1.0 ND1 A:HIS220 4.3 34.0 1.0 HE2 A:LYS127 4.3 44.5 1.0 C5 A:INS303 4.3 47.5 1.0 NE2 A:HIS123 4.3 41.0 1.0 CG A:HIS194 4.4 41.3 1.0 CB A:ASP124 4.5 40.9 1.0 ND1 A:HIS194 4.5 43.5 1.0 OD1 A:ASP195 4.6 44.6 1.0 O2 A:INS303 4.6 54.5 1.0 OD2 A:ASP253 4.6 58.0 1.0 HZ2 A:LYS127 4.7 59.8 1.0 HZ3 A:LYS127 4.8 59.8 1.0 CA A:ASP124 4.8 39.1 1.0 HB3 A:ASP124 4.9 34.1 1.0 O A:HIS123 4.9 40.5 1.0 O5 A:INS303 5.0 54.3 1.0

A.G.Thorsell, C.Persson, N.Voevodskaya, R.D.Busam, M.Hammarstrom, S.Graslund, A.Graslund, B.M.Hallberg. Structural and Biophysical Characterization of Human Myo-Inositol Oxygenase. J.Biol.Chem. V. 283 15209 2008.
ISSN: ISSN 0021-9258
PubMed: 18364358
DOI: 10.1074/JBC.M800348200