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Iron in PDB 1qhu: Mammalian Blood Serum Haemopexin Deglycosylated and in Complex with Its Ligand Haem

Protein crystallography data

The structure of Mammalian Blood Serum Haemopexin Deglycosylated and in Complex with Its Ligand Haem, PDB code: 1qhu 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 / 2.30
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 44.680, 61.950, 83.290, 90.00, 93.21, 90.00
R / Rfree (%) 20.7 / 28.9

Other elements in 1qhu:

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

Chlorine (Cl) 2 atoms
Sodium (Na) 4 atoms

Iron Binding Sites:

The binding sites of Iron atom in the Mammalian Blood Serum Haemopexin Deglycosylated and in Complex with Its Ligand Haem (pdb code 1qhu). 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 Mammalian Blood Serum Haemopexin Deglycosylated and in Complex with Its Ligand Haem, PDB code: 1qhu:

Iron binding site 1 out of 1 in 1qhu

Go back to Iron Binding Sites List in 1qhu
Iron binding site 1 out of 1 in the Mammalian Blood Serum Haemopexin Deglycosylated 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 Deglycosylated and in Complex with Its Ligand Haem within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe500

b:27.9
occ:1.00
FE A:HEM500 0.0 27.9 1.0
NC A:HEM500 2.0 29.5 1.0
ND A:HEM500 2.0 29.8 1.0
NB A:HEM500 2.0 26.7 1.0
NA A:HEM500 2.0 28.3 1.0
NE2 A:HIS213 2.2 31.8 1.0
NE2 A:HIS265 2.2 28.6 1.0
C1C A:HEM500 3.0 29.6 1.0
C4B A:HEM500 3.0 27.3 1.0
C4D A:HEM500 3.0 29.7 1.0
C1D A:HEM500 3.0 30.7 1.0
C4C A:HEM500 3.0 30.7 1.0
C1B A:HEM500 3.1 26.2 1.0
C1A A:HEM500 3.1 28.2 1.0
CE1 A:HIS213 3.1 31.1 1.0
CE1 A:HIS265 3.1 29.1 1.0
C4A A:HEM500 3.1 27.1 1.0
CD2 A:HIS213 3.1 29.4 1.0
CD2 A:HIS265 3.2 28.0 1.0
CHC A:HEM500 3.3 29.1 1.0
CHA A:HEM500 3.4 28.9 1.0
CHD A:HEM500 3.4 29.7 1.0
CHB A:HEM500 3.5 25.8 1.0
C2C A:HEM500 4.2 30.2 1.0
ND1 A:HIS213 4.2 32.3 1.0
C3D A:HEM500 4.2 32.5 1.0
C3C A:HEM500 4.2 31.2 1.0
C2D A:HEM500 4.2 31.5 1.0
ND1 A:HIS265 4.2 29.5 1.0
CG A:HIS213 4.3 31.3 1.0
C3B A:HEM500 4.3 28.0 1.0
C2B A:HEM500 4.3 28.1 1.0
C2A A:HEM500 4.3 28.6 1.0
C3A A:HEM500 4.3 27.3 1.0
CG A:HIS265 4.3 30.8 1.0

Reference:

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
Page generated: Sat Aug 3 13:26:37 2024

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