Iron in PDB 1n3u: Crystal Structure of Human Heme Oxygenase 1 (Ho-1) in Complex with Its Substrate Heme, Crystal Form B

All present enzymatic activity of Crystal Structure of Human Heme Oxygenase 1 (Ho-1) in Complex with Its Substrate Heme, Crystal Form B:
1.14.99.3;

The structure of Crystal Structure of Human Heme Oxygenase 1 (Ho-1) in Complex with Its Substrate Heme, Crystal Form B, PDB code: 1n3u was solved by L.Lad, D.J.Schuller, J.P.Friedman, H.Li, P.R.Ortiz Demontellano, T.L.Poulos, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	70.00 / 2.58
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	54.395, 55.920, 79.379, 90.00, 101.20, 90.00
R / Rfree (%)	22.5 / 26.5

The structure of Crystal Structure of Human Heme Oxygenase 1 (Ho-1) in Complex with Its Substrate Heme, Crystal Form B also contains other interesting chemical elements:

Chlorine

(Cl)

3 atoms

The binding sites of Iron atom in the Crystal Structure of Human Heme Oxygenase 1 (Ho-1) in Complex with Its Substrate Heme, Crystal Form B (pdb code 1n3u). 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 Human Heme Oxygenase 1 (Ho-1) in Complex with Its Substrate Heme, Crystal Form B, PDB code: 1n3u:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Crystal Structure of Human Heme Oxygenase 1 (Ho-1) in Complex with Its Substrate Heme, Crystal Form B


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 Human Heme Oxygenase 1 (Ho-1) in Complex with Its Substrate Heme, Crystal Form B within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe300 b:76.9 occ:1.00 FE A:HEM300 0.0 76.9 1.0 O A:HOH301 1.8 78.0 1.0 NC A:HEM300 2.0 76.7 1.0 NB A:HEM300 2.0 78.5 1.0 NA A:HEM300 2.0 79.2 1.0 ND A:HEM300 2.0 77.2 1.0 NE2 A:HIS25 2.3 76.0 1.0 C4C A:HEM300 3.0 76.5 1.0 C1C A:HEM300 3.0 76.8 1.0 C1B A:HEM300 3.1 79.5 1.0 C4B A:HEM300 3.1 78.7 1.0 C1A A:HEM300 3.1 80.2 1.0 C4A A:HEM300 3.1 80.2 1.0 C1D A:HEM300 3.1 76.3 1.0 C4D A:HEM300 3.1 77.6 1.0 CE1 A:HIS25 3.2 74.8 1.0 CD2 A:HIS25 3.3 74.0 1.0 CHD A:HEM300 3.4 76.0 1.0 CHC A:HEM300 3.4 77.7 1.0 CHA A:HEM300 3.5 78.8 1.0 CHB A:HEM300 3.5 79.8 1.0 C3C A:HEM300 4.3 76.8 1.0 C2C A:HEM300 4.3 76.8 1.0 ND1 A:HIS25 4.3 74.3 1.0 C2B A:HEM300 4.3 79.8 1.0 C3A A:HEM300 4.3 81.2 1.0 C2A A:HEM300 4.3 81.8 1.0 C3B A:HEM300 4.3 79.5 1.0 C2D A:HEM300 4.3 76.5 1.0 C3D A:HEM300 4.3 77.1 1.0 CG A:HIS25 4.4 73.0 1.0

Iron binding site 2 out of 2 in the Crystal Structure of Human Heme Oxygenase 1 (Ho-1) in Complex with Its Substrate Heme, Crystal Form B


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 Human Heme Oxygenase 1 (Ho-1) in Complex with Its Substrate Heme, Crystal Form B within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe300 b:75.9 occ:1.00 FE B:HEM300 0.0 75.9 1.0 O B:HOH301 1.8 77.2 1.0 NC B:HEM300 2.0 76.8 1.0 ND B:HEM300 2.0 76.7 1.0 NA B:HEM300 2.0 78.7 1.0 NB B:HEM300 2.0 77.5 1.0 NE2 B:HIS25 2.2 75.0 1.0 C4C B:HEM300 3.0 76.1 1.0 C1D B:HEM300 3.0 76.1 1.0 C1C B:HEM300 3.1 76.6 1.0 C1A B:HEM300 3.1 79.9 1.0 C4D B:HEM300 3.1 77.5 1.0 C4B B:HEM300 3.1 78.4 1.0 C1B B:HEM300 3.1 78.5 1.0 C4A B:HEM300 3.1 79.7 1.0 CE1 B:HIS25 3.1 73.6 1.0 CD2 B:HIS25 3.3 72.8 1.0 CHD B:HEM300 3.4 75.8 1.0 CHA B:HEM300 3.4 78.7 1.0 CHC B:HEM300 3.5 77.9 1.0 CHB B:HEM300 3.5 78.9 1.0 ND1 B:HIS25 4.2 72.3 1.0 C3C B:HEM300 4.3 76.4 1.0 C2C B:HEM300 4.3 76.3 1.0 C2D B:HEM300 4.3 76.7 1.0 C2B B:HEM300 4.3 79.2 1.0 C3D B:HEM300 4.3 77.2 1.0 C2A B:HEM300 4.3 81.6 1.0 C3A B:HEM300 4.3 80.9 1.0 CG B:HIS25 4.3 71.3 1.0 C3B B:HEM300 4.3 79.1 1.0

L.Lad, D.J.Schuller, H.Shimizu, J.Friedman, H.Li, P.R.Ortiz De Montellano, T.L.Poulos. Comparison of the Heme-Free and -Bound Crystal Structures of Human Heme Oxygenase-1 J.Biol.Chem. V. 278 7834 2003.
ISSN: ISSN 0021-9258
PubMed: 12500973
DOI: 10.1074/JBC.M211450200