Iron in PDB 1qjs: Mammalian Blood Serum Haemopexin Glycosylated-Native Protein and in Complex with Its Ligand Haem

The structure of Mammalian Blood Serum Haemopexin Glycosylated-Native Protein and in Complex with Its Ligand Haem, PDB code: 1qjs was solved by M.Paoli, H.M.Baker, W.T.Morgan, A.Smith, E.N.Baker, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 2.90
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	103.900, 69.900, 151.810, 90.00, 108.16, 90.00
R / Rfree (%)	25.5 / 31.2

The structure of Mammalian Blood Serum Haemopexin Glycosylated-Native Protein and in Complex with Its Ligand Haem also contains other interesting chemical elements:

Chlorine	(Cl)	4 atoms
Sodium	(Na)	8 atoms

The binding sites of Iron atom in the Mammalian Blood Serum Haemopexin Glycosylated-Native Protein and in Complex with Its Ligand Haem (pdb code 1qjs). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Mammalian Blood Serum Haemopexin Glycosylated-Native Protein and in Complex with Its Ligand Haem, PDB code: 1qjs:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Mammalian Blood Serum Haemopexin Glycosylated-Native Protein and in Complex with Its Ligand Haem


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Mammalian Blood Serum Haemopexin Glycosylated-Native Protein and in Complex with Its Ligand Haem within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe500 b:38.1 occ:1.00 FE A:HEM500 0.0 38.1 1.0 NA A:HEM500 2.0 28.2 1.0 NB A:HEM500 2.0 35.6 1.0 NC A:HEM500 2.1 33.4 1.0 ND A:HEM500 2.1 33.8 1.0 NE2 A:HIS213 2.4 40.4 1.0 NE2 A:HIS266 2.4 37.5 1.0 C1A A:HEM500 3.0 26.9 1.0 C4D A:HEM500 3.0 34.8 1.0 C4B A:HEM500 3.0 39.6 1.0 C4A A:HEM500 3.0 25.2 1.0 CD2 A:HIS213 3.0 38.6 1.0 C1C A:HEM500 3.0 35.5 1.0 C4C A:HEM500 3.1 32.2 1.0 C1B A:HEM500 3.1 34.0 1.0 C1D A:HEM500 3.1 33.2 1.0 CHA A:HEM500 3.3 30.0 1.0 CHC A:HEM500 3.4 37.6 1.0 CHB A:HEM500 3.4 27.8 1.0 CD2 A:HIS266 3.4 37.5 1.0 CHD A:HEM500 3.4 33.2 1.0 CE1 A:HIS266 3.4 38.7 1.0 CE1 A:HIS213 3.6 41.1 1.0 C2A A:HEM500 4.2 30.9 1.0 C3A A:HEM500 4.2 28.0 1.0 C3B A:HEM500 4.2 36.6 1.0 C2C A:HEM500 4.3 36.2 1.0 C3D A:HEM500 4.3 33.7 1.0 C3C A:HEM500 4.3 31.7 1.0 C2D A:HEM500 4.3 33.4 1.0 C2B A:HEM500 4.3 35.9 1.0 CG A:HIS213 4.3 44.1 1.0 ND1 A:HIS213 4.6 37.9 1.0 ND1 A:HIS266 4.6 32.6 1.0 CG A:HIS266 4.6 34.0 1.0

Iron binding site 2 out of 2 in the Mammalian Blood Serum Haemopexin Glycosylated-Native Protein and in Complex with Its Ligand Haem


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Mammalian Blood Serum Haemopexin Glycosylated-Native Protein and in Complex with Its Ligand Haem within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe500 b:29.6 occ:1.00 FE B:HEM500 0.0 29.6 1.0 NE2 B:HIS213 1.7 33.6 1.0 NA B:HEM500 2.1 30.3 1.0 NC B:HEM500 2.1 29.4 1.0 NB B:HEM500 2.1 23.8 1.0 ND B:HEM500 2.2 29.5 1.0 CD2 B:HIS213 2.6 36.2 1.0 CE1 B:HIS213 2.8 40.9 1.0 C4A B:HEM500 3.0 28.3 1.0 C1C B:HEM500 3.0 29.1 1.0 C1A B:HEM500 3.0 32.6 1.0 C4C B:HEM500 3.1 32.4 1.0 C4B B:HEM500 3.1 21.4 1.0 C1D B:HEM500 3.1 35.3 1.0 C4D B:HEM500 3.2 30.8 1.0 C1B B:HEM500 3.2 20.5 1.0 NE2 B:HIS266 3.4 28.7 1.0 CHA B:HEM500 3.4 30.1 1.0 CHD B:HEM500 3.4 33.1 1.0 CHC B:HEM500 3.4 21.8 1.0 CHB B:HEM500 3.5 24.7 1.0 CG B:HIS213 3.8 37.7 1.0 ND1 B:HIS213 3.9 38.5 1.0 CD2 B:HIS266 4.0 29.9 1.0 C3A B:HEM500 4.2 29.1 1.0 C2A B:HEM500 4.2 31.7 1.0 C2C B:HEM500 4.3 34.9 1.0 C3C B:HEM500 4.3 36.1 1.0 C3B B:HEM500 4.3 21.4 1.0 C2D B:HEM500 4.4 36.8 1.0 C2B B:HEM500 4.4 18.6 1.0 C3D B:HEM500 4.4 35.5 1.0 CE1 B:HIS266 4.5 25.8 1.0 CD1 B:TYR204 4.9 30.9 1.0

M.Paoli, B.F.Anderson, H.M.Baker, W.T.Morgan, A.Smith, E.N.Baker. Crystal Structure of Hemopexin Reveals A Novel High-Affinity Heme Site Formed Between Two Beta-Propeller Domains. Nat.Struct.Biol. V. 6 926 1999.
ISSN: ISSN 1072-8368
PubMed: 10504726
DOI: 10.1038/13294