Iron in PDB 1wow: Crystal Structure of Heme Oxygenase-2 From Synechocystis Sp. Pcc 6803 Complexed with Heme in Ferrous Form

All present enzymatic activity of Crystal Structure of Heme Oxygenase-2 From Synechocystis Sp. Pcc 6803 Complexed with Heme in Ferrous Form:
1.14.99.3;

The structure of Crystal Structure of Heme Oxygenase-2 From Synechocystis Sp. Pcc 6803 Complexed with Heme in Ferrous Form, PDB code: 1wow was solved by M.Sugishima, Y.Hagiwara, X.Zhang, T.Yoshida, C.T.Migita, K.Fukuyama, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 2.20
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	58.030, 74.280, 72.270, 90.00, 108.03, 90.00
R / Rfree (%)	21.9 / 28.2

The binding sites of Iron atom in the Crystal Structure of Heme Oxygenase-2 From Synechocystis Sp. Pcc 6803 Complexed with Heme in Ferrous Form (pdb code 1wow). 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 Heme Oxygenase-2 From Synechocystis Sp. Pcc 6803 Complexed with Heme in Ferrous Form, PDB code: 1wow:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Crystal Structure of Heme Oxygenase-2 From Synechocystis Sp. Pcc 6803 Complexed with Heme in Ferrous Form


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 Heme Oxygenase-2 From Synechocystis Sp. Pcc 6803 Complexed with Heme in Ferrous Form within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe300 b:13.8 occ:1.00 FE A:HEM300 0.0 13.8 1.0 ND A:HEM300 2.0 11.6 1.0 NB A:HEM300 2.0 11.6 1.0 NC A:HEM300 2.0 12.3 1.0 NA A:HEM300 2.0 11.8 1.0 NE2 A:HIS16 2.2 14.8 1.0 C4D A:HEM300 3.0 11.9 1.0 C1D A:HEM300 3.0 11.5 1.0 C1B A:HEM300 3.0 13.3 1.0 C1A A:HEM300 3.0 14.9 1.0 C4B A:HEM300 3.0 13.3 1.0 C4C A:HEM300 3.0 12.8 1.0 C4A A:HEM300 3.1 12.2 1.0 C1C A:HEM300 3.1 11.0 1.0 CD2 A:HIS16 3.1 16.0 1.0 CE1 A:HIS16 3.3 15.5 1.0 CHA A:HEM300 3.4 11.4 1.0 CHD A:HEM300 3.4 8.6 1.0 CHC A:HEM300 3.4 12.7 1.0 CHB A:HEM300 3.4 11.6 1.0 C3D A:HEM300 4.3 13.2 1.0 C2D A:HEM300 4.3 12.6 1.0 C2B A:HEM300 4.3 15.7 1.0 C2A A:HEM300 4.3 14.3 1.0 C3C A:HEM300 4.3 11.6 1.0 C3B A:HEM300 4.3 15.4 1.0 C2C A:HEM300 4.3 12.6 1.0 C3A A:HEM300 4.3 13.1 1.0 CG A:HIS16 4.3 13.8 1.0 ND1 A:HIS16 4.4 15.5 1.0 N A:GLY133 4.4 18.8 1.0 CA A:GLY133 4.6 18.0 1.0 CA A:GLY129 4.7 16.1 1.0 O A:GLY129 4.9 17.1 1.0

Iron binding site 2 out of 2 in the Crystal Structure of Heme Oxygenase-2 From Synechocystis Sp. Pcc 6803 Complexed with Heme in Ferrous Form


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 Heme Oxygenase-2 From Synechocystis Sp. Pcc 6803 Complexed with Heme in Ferrous Form within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe300 b:18.4 occ:1.00 FE B:HEM300 0.0 18.4 1.0 ND B:HEM300 2.0 17.4 1.0 NB B:HEM300 2.0 18.7 1.0 NC B:HEM300 2.0 17.1 1.0 NA B:HEM300 2.0 16.9 1.0 NE2 B:HIS16 2.1 17.0 1.0 C4D B:HEM300 3.0 18.1 1.0 C1D B:HEM300 3.0 17.8 1.0 C1B B:HEM300 3.0 18.0 1.0 C1A B:HEM300 3.0 16.4 1.0 C4A B:HEM300 3.0 17.8 1.0 C4B B:HEM300 3.1 17.3 1.0 C4C B:HEM300 3.1 17.1 1.0 C1C B:HEM300 3.1 16.0 1.0 CD2 B:HIS16 3.1 15.1 1.0 CE1 B:HIS16 3.1 18.2 1.0 CHA B:HEM300 3.4 16.3 1.0 CHD B:HEM300 3.4 15.5 1.0 CHC B:HEM300 3.4 16.9 1.0 CHB B:HEM300 3.4 17.1 1.0 O B:HOH480 3.9 39.5 1.0 ND1 B:HIS16 4.2 15.9 1.0 N B:GLY133 4.2 19.7 1.0 CG B:HIS16 4.3 15.2 1.0 C3D B:HEM300 4.3 18.1 1.0 C2A B:HEM300 4.3 18.4 1.0 C2B B:HEM300 4.3 18.4 1.0 C3A B:HEM300 4.3 17.3 1.0 C2D B:HEM300 4.3 18.8 1.0 C3C B:HEM300 4.3 14.9 1.0 C3B B:HEM300 4.3 18.6 1.0 C2C B:HEM300 4.3 15.3 1.0 CA B:GLY133 4.5 18.3 1.0 CA B:GLY129 4.7 14.7 1.0 CB B:SER132 4.8 18.1 1.0 O B:GLY129 4.9 15.2 1.0 CG2 B:THR234 5.0 22.5 1.0

M.Sugishima, Y.Hagiwara, X.Zhang, T.Yoshida, C.T.Migita, K.Fukuyama. Crystal Structure of Dimeric Heme Oxygenase-2 From Synechocystis Sp. Pcc 6803 in Complex with Heme. Biochemistry V. 44 4257 2005.
ISSN: ISSN 0006-2960
PubMed: 15766254
DOI: 10.1021/BI0480483