Iron in PDB 1moh: Ferric Monomeric Hemoglobin I (Hb I)

The structure of Ferric Monomeric Hemoglobin I (Hb I), PDB code: 1moh was solved by M.Rizzi, J.B.Wittenberg, P.Ascenzi, M.Bolognesi, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	15.00 / 1.90
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	50.550, 38.790, 42.510, 90.00, 106.93, 90.00
R / Rfree (%)	18.6 / n/a

The binding sites of Iron atom in the Ferric Monomeric Hemoglobin I (Hb I) (pdb code 1moh). 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 Ferric Monomeric Hemoglobin I (Hb I), PDB code: 1moh:

Iron binding site 1 out of 1 in the Ferric Monomeric Hemoglobin I (Hb I)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Ferric Monomeric Hemoglobin I (Hb I) within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe143 b:20.1 occ:1.00 FE A:HEM143 0.0 20.1 1.0 NC A:HEM143 1.7 10.2 1.0 NA A:HEM143 1.7 13.5 1.0 ND A:HEM143 2.0 19.2 1.0 NB A:HEM143 2.1 17.6 1.0 NE2 A:HIS96 2.1 18.5 1.0 S A:H2S1154 2.3 28.2 1.0 C1C A:HEM143 2.8 17.2 1.0 C1A A:HEM143 2.8 22.8 1.0 C4C A:HEM143 2.9 20.3 1.0 C4A A:HEM143 2.9 20.9 1.0 C1D A:HEM143 3.0 19.2 1.0 C4D A:HEM143 3.0 13.9 1.0 C1B A:HEM143 3.0 13.3 1.0 CE1 A:HIS96 3.1 20.6 1.0 C4B A:HEM143 3.1 17.8 1.0 CD2 A:HIS96 3.1 18.7 1.0 CHA A:HEM143 3.3 18.1 1.0 CHC A:HEM143 3.3 22.1 1.0 CHB A:HEM143 3.4 20.3 1.0 CHD A:HEM143 3.4 28.1 1.0 C2A A:HEM143 4.1 22.3 1.0 C2C A:HEM143 4.1 21.8 1.0 C3A A:HEM143 4.1 21.6 1.0 C3C A:HEM143 4.1 21.5 1.0 ND1 A:HIS96 4.2 19.0 1.0 C2D A:HEM143 4.2 20.1 1.0 C3D A:HEM143 4.3 21.6 1.0 C2B A:HEM143 4.3 14.6 1.0 CG A:HIS96 4.3 19.2 1.0 C3B A:HEM143 4.4 25.4 1.0 OE1 A:GLN64 4.7 27.6 1.0 CE1 A:PHE92 4.7 25.4 1.0 NH1 A:ARG99 4.9 24.1 1.0

M.Rizzi, J.B.Wittenberg, A.Coda, P.Ascenzi, M.Bolognesi. Structural Bases For Sulfide Recognition in Lucina Pectinata Hemoglobin I. J.Mol.Biol. V. 258 1 1996.
ISSN: ISSN 0022-2836
PubMed: 8613980
DOI: 10.1006/JMBI.1996.0228