Iron in PDB 5lfg: X-Ray Structure of A New Fully Ligated Carbomonoxy Form of Trematomus Newnesi Hemoglobin (HB1TNCO).

The structure of X-Ray Structure of A New Fully Ligated Carbomonoxy Form of Trematomus Newnesi Hemoglobin (HB1TNCO)., PDB code: 5lfg was solved by L.Vitagliano, L.Mazzarella, A.Merlino, A.Vergara, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	8.00 / 1.94
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	86.206, 87.256, 109.648, 90.00, 101.81, 90.00
R / Rfree (%)	n/a / 24.5

The binding sites of Iron atom in the X-Ray Structure of A New Fully Ligated Carbomonoxy Form of Trematomus Newnesi Hemoglobin (HB1TNCO). (pdb code 5lfg). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 4 binding sites of Iron where determined in the X-Ray Structure of A New Fully Ligated Carbomonoxy Form of Trematomus Newnesi Hemoglobin (HB1TNCO)., PDB code: 5lfg:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in the X-Ray Structure of A New Fully Ligated Carbomonoxy Form of Trematomus Newnesi Hemoglobin (HB1TNCO).


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of X-Ray Structure of A New Fully Ligated Carbomonoxy Form of Trematomus Newnesi Hemoglobin (HB1TNCO). within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe202 b:27.4 occ:1.00 FE A:HEM202 0.0 27.4 1.0 C A:CMO201 1.9 30.5 1.0 ND A:HEM202 2.0 27.7 1.0 NA A:HEM202 2.0 25.0 1.0 NC A:HEM202 2.0 22.6 1.0 NB A:HEM202 2.0 22.6 1.0 NE2 A:HIS88 2.1 25.0 1.0 O A:CMO201 3.0 26.5 1.0 CE1 A:HIS88 3.0 22.9 1.0 C1A A:HEM202 3.0 25.9 1.0 C4D A:HEM202 3.0 26.5 1.0 C4C A:HEM202 3.0 23.6 1.0 C1C A:HEM202 3.0 23.1 1.0 C1D A:HEM202 3.0 28.5 1.0 C4A A:HEM202 3.0 23.4 1.0 C4B A:HEM202 3.1 24.6 1.0 C1B A:HEM202 3.1 19.9 1.0 CD2 A:HIS88 3.2 25.2 1.0 CHA A:HEM202 3.4 24.4 1.0 CHD A:HEM202 3.4 25.6 1.0 CHC A:HEM202 3.4 24.7 1.0 CHB A:HEM202 3.4 20.4 1.0 ND1 A:HIS88 4.2 22.1 1.0 C2A A:HEM202 4.3 26.2 1.0 C3D A:HEM202 4.3 27.6 1.0 C2D A:HEM202 4.3 26.2 1.0 C3C A:HEM202 4.3 22.4 1.0 C2C A:HEM202 4.3 22.8 1.0 C3A A:HEM202 4.3 23.1 1.0 C3B A:HEM202 4.3 25.0 1.0 C2B A:HEM202 4.3 23.2 1.0 CG A:HIS88 4.3 23.1 1.0 NE2 A:HIS59 4.4 32.6 1.0 CG2 A:VAL63 4.8 27.0 1.0

Iron binding site 2 out of 4 in the X-Ray Structure of A New Fully Ligated Carbomonoxy Form of Trematomus Newnesi Hemoglobin (HB1TNCO).


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of X-Ray Structure of A New Fully Ligated Carbomonoxy Form of Trematomus Newnesi Hemoglobin (HB1TNCO). within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe202 b:29.1 occ:1.00 FE B:HEM202 0.0 29.1 1.0 C B:CMO201 1.8 33.0 1.0 NA B:HEM202 2.0 36.1 1.0 NC B:HEM202 2.0 25.3 1.0 ND B:HEM202 2.0 29.3 1.0 NB B:HEM202 2.0 24.5 1.0 NE2 B:HIS92 2.1 23.3 1.0 O B:CMO201 2.9 35.9 1.0 CD2 B:HIS92 3.0 22.9 1.0 C1A B:HEM202 3.0 35.3 1.0 C4D B:HEM202 3.0 30.8 1.0 C1D B:HEM202 3.0 30.3 1.0 C1C B:HEM202 3.0 24.1 1.0 C4A B:HEM202 3.0 35.9 1.0 C4C B:HEM202 3.0 27.5 1.0 C1B B:HEM202 3.1 28.0 1.0 C4B B:HEM202 3.1 22.9 1.0 CE1 B:HIS92 3.2 24.9 1.0 CHA B:HEM202 3.4 32.8 1.0 CHD B:HEM202 3.4 28.1 1.0 CHC B:HEM202 3.4 21.6 1.0 CHB B:HEM202 3.4 33.2 1.0 CG B:HIS92 4.2 23.3 1.0 C2A B:HEM202 4.2 36.5 1.0 C3A B:HEM202 4.3 35.9 1.0 C3D B:HEM202 4.3 33.5 1.0 ND1 B:HIS92 4.3 25.1 1.0 C2D B:HEM202 4.3 31.3 1.0 C3C B:HEM202 4.3 26.4 1.0 C2C B:HEM202 4.3 25.4 1.0 C2B B:HEM202 4.3 23.6 1.0 C3B B:HEM202 4.3 24.4 1.0 CG2 B:VAL67 4.5 24.0 1.0

Iron binding site 3 out of 4 in the X-Ray Structure of A New Fully Ligated Carbomonoxy Form of Trematomus Newnesi Hemoglobin (HB1TNCO).


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of X-Ray Structure of A New Fully Ligated Carbomonoxy Form of Trematomus Newnesi Hemoglobin (HB1TNCO). within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe202 b:28.3 occ:1.00 FE C:HEM202 0.0 28.3 1.0 C C:CMO201 1.8 38.9 1.0 NA C:HEM202 2.0 32.6 1.0 ND C:HEM202 2.0 28.4 1.0 NB C:HEM202 2.0 23.3 1.0 NC C:HEM202 2.0 22.6 1.0 NE2 C:HIS88 2.2 25.4 1.0 O C:CMO201 3.0 40.0 1.0 C1A C:HEM202 3.0 33.6 1.0 C4A C:HEM202 3.0 33.5 1.0 C1D C:HEM202 3.0 28.6 1.0 C4D C:HEM202 3.0 30.5 1.0 C4C C:HEM202 3.0 26.9 1.0 C1B C:HEM202 3.1 27.4 1.0 C4B C:HEM202 3.1 23.1 1.0 C1C C:HEM202 3.1 24.5 1.0 CE1 C:HIS88 3.1 24.8 1.0 CD2 C:HIS88 3.2 27.7 1.0 CHA C:HEM202 3.4 32.0 1.0 CHB C:HEM202 3.4 30.2 1.0 CHD C:HEM202 3.4 26.8 1.0 CHC C:HEM202 3.4 22.5 1.0 C2A C:HEM202 4.2 36.2 1.0 ND1 C:HIS88 4.2 28.3 1.0 C3A C:HEM202 4.2 35.2 1.0 C3D C:HEM202 4.3 29.9 1.0 C2D C:HEM202 4.3 30.2 1.0 C2B C:HEM202 4.3 25.9 1.0 C3B C:HEM202 4.3 25.2 1.0 C3C C:HEM202 4.3 26.6 1.0 C2C C:HEM202 4.3 25.5 1.0 CG C:HIS88 4.3 29.6 1.0 CG2 C:VAL63 4.6 16.4 1.0

Iron binding site 4 out of 4 in the X-Ray Structure of A New Fully Ligated Carbomonoxy Form of Trematomus Newnesi Hemoglobin (HB1TNCO).


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of X-Ray Structure of A New Fully Ligated Carbomonoxy Form of Trematomus Newnesi Hemoglobin (HB1TNCO). within 5.0Å range: probe atom residue distance (Å) B Occ D:Fe201 b:33.3 occ:1.00 FE D:HEM201 0.0 33.3 1.0 C D:CMO202 1.6 25.9 1.0 NA D:HEM201 2.0 35.3 1.0 NB D:HEM201 2.0 27.0 1.0 NC D:HEM201 2.0 27.2 1.0 ND D:HEM201 2.0 28.7 1.0 NE2 D:HIS92 2.1 32.6 1.0 O D:CMO202 2.6 27.0 1.0 CE1 D:HIS92 2.9 31.0 1.0 C1A D:HEM201 3.0 37.5 1.0 C1B D:HEM201 3.0 30.5 1.0 C4B D:HEM201 3.0 26.3 1.0 C4A D:HEM201 3.0 35.7 1.0 C4C D:HEM201 3.0 25.1 1.0 C1C D:HEM201 3.0 27.7 1.0 C1D D:HEM201 3.1 28.5 1.0 C4D D:HEM201 3.1 32.9 1.0 CD2 D:HIS92 3.1 32.2 1.0 CHA D:HEM201 3.4 35.0 1.0 CHB D:HEM201 3.4 33.5 1.0 CHC D:HEM201 3.4 23.2 1.0 CHD D:HEM201 3.4 27.2 1.0 ND1 D:HIS92 4.1 30.5 1.0 CG D:HIS92 4.2 30.8 1.0 C2A D:HEM201 4.3 41.5 1.0 C2B D:HEM201 4.3 28.9 1.0 C3A D:HEM201 4.3 40.1 1.0 C3B D:HEM201 4.3 28.0 1.0 C3C D:HEM201 4.3 25.8 1.0 C2C D:HEM201 4.3 28.4 1.0 C2D D:HEM201 4.3 32.2 1.0 C3D D:HEM201 4.3 35.9 1.0 CG2 D:VAL67 4.4 21.4 1.0

L.Vitagliano, L.Mazzarella, A.Merlino, A.Vergara. Fine Sampling of the Rt Quaternary-Structure Transition of A Tetrameric Hemoglobin. Chemistry V. 23 605 2017.
ISSN: ISSN 1521-3765
PubMed: 27808442
DOI: 10.1002/CHEM.201603421