Iron in PDB 4rom: Deoxyhemoglobin in Complex with Imidazolylacryloyl Derivatives

The structure of Deoxyhemoglobin in Complex with Imidazolylacryloyl Derivatives, PDB code: 4rom was solved by A.M.Omar, M.A.Mahran, M.N.Ghatge, N.Chowdhury, F.H.A.Bamane, M.E.El-Araby, O.Abdulmalik, M.K.Safo, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	33.18 / 1.90
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	61.985, 78.922, 53.264, 90.00, 98.44, 90.00
R / Rfree (%)	21.3 / 24.8

The structure of Deoxyhemoglobin in Complex with Imidazolylacryloyl Derivatives also contains other interesting chemical elements:

Chlorine

(Cl)

2 atoms

The binding sites of Iron atom in the Deoxyhemoglobin in Complex with Imidazolylacryloyl Derivatives (pdb code 4rom). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 4 binding sites of Iron where determined in the Deoxyhemoglobin in Complex with Imidazolylacryloyl Derivatives, PDB code: 4rom:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in the Deoxyhemoglobin in Complex with Imidazolylacryloyl Derivatives


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Deoxyhemoglobin in Complex with Imidazolylacryloyl Derivatives within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe201 b:20.1 occ:1.00 FE A:HEM201 0.0 20.1 1.0 ND A:HEM201 2.0 19.4 1.0 NB A:HEM201 2.0 20.3 1.0 NA A:HEM201 2.0 20.7 1.0 NC A:HEM201 2.0 18.5 1.0 NE2 A:HIS87 2.1 19.2 1.0 CE1 A:HIS87 2.9 19.9 1.0 C4B A:HEM201 3.0 20.0 1.0 C4D A:HEM201 3.1 19.6 1.0 C1C A:HEM201 3.1 19.2 1.0 C1A A:HEM201 3.1 21.4 1.0 C1D A:HEM201 3.1 18.6 1.0 C4A A:HEM201 3.1 21.1 1.0 C1B A:HEM201 3.1 20.6 1.0 C4C A:HEM201 3.1 18.1 1.0 CD2 A:HIS87 3.1 19.4 1.0 CHC A:HEM201 3.4 19.6 1.0 CHA A:HEM201 3.4 19.2 1.0 CHD A:HEM201 3.5 17.6 1.0 CHB A:HEM201 3.5 19.7 1.0 O A:HOH410 3.6 20.1 1.0 ND1 A:HIS87 4.1 19.4 1.0 CG A:HIS87 4.2 20.2 1.0 C2D A:HEM201 4.3 19.5 1.0 C3D A:HEM201 4.3 19.6 1.0 C3B A:HEM201 4.3 21.0 1.0 C2A A:HEM201 4.3 22.3 1.0 C2B A:HEM201 4.3 20.9 1.0 C2C A:HEM201 4.3 18.7 1.0 CE1 A:HIS58 4.3 24.8 1.0 C3A A:HEM201 4.3 22.1 1.0 C3C A:HEM201 4.4 18.1 1.0 CD1 A:LEU91 4.5 20.4 1.0 NE2 A:HIS58 4.6 25.7 1.0

Iron binding site 2 out of 4 in the Deoxyhemoglobin in Complex with Imidazolylacryloyl Derivatives


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Deoxyhemoglobin in Complex with Imidazolylacryloyl Derivatives within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe201 b:22.9 occ:1.00 FE B:HEM201 0.0 22.9 1.0 NB B:HEM201 2.0 22.1 1.0 ND B:HEM201 2.0 22.8 1.0 NA B:HEM201 2.0 23.7 1.0 NC B:HEM201 2.0 21.2 1.0 NE2 B:HIS92 2.1 23.4 1.0 CE1 B:HIS92 3.0 22.9 1.0 C4B B:HEM201 3.0 22.6 1.0 C1B B:HEM201 3.0 22.1 1.0 C1D B:HEM201 3.1 22.3 1.0 C4D B:HEM201 3.1 23.0 1.0 CD2 B:HIS92 3.1 23.6 1.0 C4A B:HEM201 3.1 23.1 1.0 C1A B:HEM201 3.1 24.1 1.0 C1C B:HEM201 3.1 21.0 1.0 C4C B:HEM201 3.1 21.1 1.0 CHC B:HEM201 3.4 21.9 1.0 CHB B:HEM201 3.5 22.3 1.0 CHA B:HEM201 3.5 23.2 1.0 CHD B:HEM201 3.5 20.9 1.0 CG2 B:VAL67 4.1 31.6 1.0 ND1 B:HIS92 4.1 25.1 1.0 NE2 B:HIS63 4.1 32.3 1.0 CG B:HIS92 4.2 24.7 1.0 C3B B:HEM201 4.3 22.4 1.0 C2B B:HEM201 4.3 22.7 1.0 C2D B:HEM201 4.3 22.4 1.0 C2A B:HEM201 4.3 24.4 1.0 C3D B:HEM201 4.3 22.9 1.0 C3A B:HEM201 4.3 24.6 1.0 C2C B:HEM201 4.4 21.3 1.0 C3C B:HEM201 4.4 20.3 1.0 CE1 B:HIS63 4.4 32.5 1.0 CE1 B:PHE103 4.9 22.9 1.0 CD1 B:LEU96 5.0 25.4 1.0

Iron binding site 3 out of 4 in the Deoxyhemoglobin in Complex with Imidazolylacryloyl Derivatives


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Deoxyhemoglobin in Complex with Imidazolylacryloyl Derivatives within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe201 b:22.2 occ:1.00 FE C:HEM201 0.0 22.2 1.0 ND C:HEM201 2.0 22.2 1.0 NB C:HEM201 2.0 21.8 1.0 NC C:HEM201 2.0 20.2 1.0 NE2 C:HIS87 2.0 23.4 1.0 NA C:HEM201 2.0 22.8 1.0 CE1 C:HIS87 3.0 24.4 1.0 C4B C:HEM201 3.1 20.9 1.0 C1D C:HEM201 3.1 21.4 1.0 C4D C:HEM201 3.1 22.8 1.0 C1C C:HEM201 3.1 21.0 1.0 C1A C:HEM201 3.1 23.6 1.0 C1B C:HEM201 3.1 22.0 1.0 C4C C:HEM201 3.1 20.9 1.0 CD2 C:HIS87 3.1 24.4 1.0 C4A C:HEM201 3.1 23.7 1.0 CHC C:HEM201 3.4 20.3 1.0 CHA C:HEM201 3.4 23.1 1.0 CHD C:HEM201 3.5 20.4 1.0 CHB C:HEM201 3.5 22.1 1.0 O C:HOH430 3.7 39.0 1.0 NE2 C:HIS58 4.0 28.6 1.0 ND1 C:HIS87 4.1 24.4 1.0 CG C:HIS87 4.2 24.6 1.0 C2D C:HEM201 4.3 22.4 1.0 C3B C:HEM201 4.3 21.2 1.0 C3D C:HEM201 4.3 22.7 1.0 C2B C:HEM201 4.3 21.2 1.0 C2A C:HEM201 4.3 25.1 1.0 C2C C:HEM201 4.3 20.1 1.0 C3A C:HEM201 4.4 24.3 1.0 C3C C:HEM201 4.4 20.0 1.0 CE1 C:HIS58 4.5 26.3 1.0 CD1 C:LEU91 4.5 27.4 1.0

Iron binding site 4 out of 4 in the Deoxyhemoglobin in Complex with Imidazolylacryloyl Derivatives


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Deoxyhemoglobin in Complex with Imidazolylacryloyl Derivatives within 5.0Å range: probe atom residue distance (Å) B Occ D:Fe201 b:24.7 occ:1.00 FE D:HEM201 0.0 24.7 1.0 NB D:HEM201 2.0 25.0 1.0 ND D:HEM201 2.0 25.5 1.0 NA D:HEM201 2.0 26.4 1.0 NE2 D:HIS92 2.0 24.4 1.0 NC D:HEM201 2.0 24.3 1.0 CE1 D:HIS92 3.0 24.6 1.0 C1B D:HEM201 3.0 25.1 1.0 C4B D:HEM201 3.0 24.9 1.0 C4A D:HEM201 3.1 26.5 1.0 C1D D:HEM201 3.1 25.5 1.0 C4D D:HEM201 3.1 26.4 1.0 C1A D:HEM201 3.1 27.7 1.0 CD2 D:HIS92 3.1 24.4 1.0 C1C D:HEM201 3.1 23.4 1.0 C4C D:HEM201 3.1 23.4 1.0 CHC D:HEM201 3.4 24.4 1.0 CHB D:HEM201 3.4 25.8 1.0 CHA D:HEM201 3.5 26.9 1.0 CHD D:HEM201 3.5 23.9 1.0 ND1 D:HIS92 4.1 25.1 1.0 CG D:HIS92 4.2 24.7 1.0 C2B D:HEM201 4.3 25.8 1.0 C3A D:HEM201 4.3 28.5 1.0 C3B D:HEM201 4.3 25.9 1.0 C2A D:HEM201 4.3 29.3 1.0 C3D D:HEM201 4.3 27.3 1.0 C2D D:HEM201 4.3 26.4 1.0 C2C D:HEM201 4.4 24.0 1.0 C3C D:HEM201 4.4 23.4 1.0 CG2 D:VAL67 4.4 29.3 1.0 CE1 D:HIS63 4.4 29.4 1.0 NE2 D:HIS63 4.6 29.9 1.0 CD1 D:LEU96 4.7 27.7 1.0

A.M.Omar, M.A.Mahran, M.N.Ghatge, N.Chowdhury, F.H.A.Bamane, M.E.El-Araby, O.Abdulmalik, M.K.Safo. Identification of A Novel Class of Covalent Modifiers of Hemoglobin As Potential Antisickling Agents Org.Biomol.Chem. 2015.
ISSN: ESSN 1477-0539