Iron in PDB 4g51: Crystallographic Analysis of the Interaction of Nitric Oxide with Hemoglobin From Trematomus Bernacchii in the T Quaternary Structure (Fully Ligated State).

The structure of Crystallographic Analysis of the Interaction of Nitric Oxide with Hemoglobin From Trematomus Bernacchii in the T Quaternary Structure (Fully Ligated State)., PDB code: 4g51 was solved by A.Merlino, A.Balsamo, A.Pica, L.Mazzarella, A.Vergara, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.00 / 2.50
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	62.002, 94.672, 61.956, 90.00, 89.16, 90.00
R / Rfree (%)	18.1 / 24.9

The binding sites of Iron atom in the Crystallographic Analysis of the Interaction of Nitric Oxide with Hemoglobin From Trematomus Bernacchii in the T Quaternary Structure (Fully Ligated State). (pdb code 4g51). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 4 binding sites of Iron where determined in the Crystallographic Analysis of the Interaction of Nitric Oxide with Hemoglobin From Trematomus Bernacchii in the T Quaternary Structure (Fully Ligated State)., PDB code: 4g51:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in the Crystallographic Analysis of the Interaction of Nitric Oxide with Hemoglobin From Trematomus Bernacchii in the T Quaternary Structure (Fully Ligated State).


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Crystallographic Analysis of the Interaction of Nitric Oxide with Hemoglobin From Trematomus Bernacchii in the T Quaternary Structure (Fully Ligated State). within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe202 b:38.5 occ:1.00 FE A:HEM202 0.0 38.5 1.0 N A:NO201 1.8 38.3 1.0 ND A:HEM202 2.0 18.9 1.0 NA A:HEM202 2.0 40.7 1.0 NB A:HEM202 2.0 18.9 1.0 NC A:HEM202 2.0 7.5 1.0 NE2 A:HIS88 2.1 39.9 1.0 O A:NO201 3.0 54.2 1.0 CD2 A:HIS88 3.0 40.2 1.0 C1D A:HEM202 3.0 12.0 1.0 C4D A:HEM202 3.0 29.9 1.0 C1A A:HEM202 3.1 43.6 1.0 C4C A:HEM202 3.1 7.0 1.0 C4A A:HEM202 3.1 38.2 1.0 C1B A:HEM202 3.1 25.5 1.0 C1C A:HEM202 3.1 12.3 1.0 C4B A:HEM202 3.1 25.2 1.0 CE1 A:HIS88 3.1 39.1 1.0 CHA A:HEM202 3.4 37.7 1.0 CHD A:HEM202 3.4 8.0 1.0 CHB A:HEM202 3.4 34.5 1.0 CHC A:HEM202 3.4 20.9 1.0 CG A:HIS88 4.2 36.8 1.0 ND1 A:HIS88 4.2 39.0 1.0 C2D A:HEM202 4.3 20.5 1.0 C3D A:HEM202 4.3 22.2 1.0 C3A A:HEM202 4.3 43.2 1.0 C2A A:HEM202 4.3 46.5 1.0 C3C A:HEM202 4.3 12.7 1.0 C2B A:HEM202 4.3 25.5 1.0 C2C A:HEM202 4.3 14.3 1.0 C3B A:HEM202 4.3 25.2 1.0 NE2 A:HIS59 4.8 49.8 1.0 CG2 A:VAL63 5.0 31.3 1.0 CD1 A:LEU92 5.0 20.5 1.0

Iron binding site 2 out of 4 in the Crystallographic Analysis of the Interaction of Nitric Oxide with Hemoglobin From Trematomus Bernacchii in the T Quaternary Structure (Fully Ligated State).


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Crystallographic Analysis of the Interaction of Nitric Oxide with Hemoglobin From Trematomus Bernacchii in the T Quaternary Structure (Fully Ligated State). within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe202 b:41.3 occ:1.00 FE B:HEM202 0.0 41.3 1.0 N B:NO201 1.8 52.1 1.0 NB B:HEM202 2.0 33.7 1.0 NA B:HEM202 2.0 38.2 1.0 NC B:HEM202 2.0 45.2 1.0 ND B:HEM202 2.0 37.3 1.0 NE2 B:HIS92 2.1 50.9 1.0 CE1 B:HIS92 2.8 49.8 1.0 O B:NO201 3.0 46.3 1.0 C1C B:HEM202 3.0 45.7 1.0 C1A B:HEM202 3.0 40.8 1.0 C4C B:HEM202 3.0 40.4 1.0 C4A B:HEM202 3.0 41.2 1.0 C1B B:HEM202 3.0 37.9 1.0 C4B B:HEM202 3.1 37.6 1.0 C4D B:HEM202 3.1 39.8 1.0 C1D B:HEM202 3.1 36.3 1.0 CD2 B:HIS92 3.3 50.4 1.0 CHC B:HEM202 3.4 39.0 1.0 CHA B:HEM202 3.4 40.5 1.0 CHB B:HEM202 3.4 40.2 1.0 CHD B:HEM202 3.4 34.5 1.0 ND1 B:HIS92 4.0 46.8 1.0 NE2 B:HIS63 4.0 34.5 1.0 C2C B:HEM202 4.2 49.1 1.0 C2A B:HEM202 4.2 43.0 1.0 C3C B:HEM202 4.2 47.1 1.0 C3A B:HEM202 4.2 43.4 1.0 CG B:HIS92 4.2 48.5 1.0 C2B B:HEM202 4.3 39.9 1.0 C3B B:HEM202 4.3 38.8 1.0 C3D B:HEM202 4.3 43.9 1.0 C2D B:HEM202 4.3 41.1 1.0 CE1 B:HIS63 4.7 27.4 1.0 CG2 B:VAL67 4.8 21.1 1.0

Iron binding site 3 out of 4 in the Crystallographic Analysis of the Interaction of Nitric Oxide with Hemoglobin From Trematomus Bernacchii in the T Quaternary Structure (Fully Ligated State).


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Crystallographic Analysis of the Interaction of Nitric Oxide with Hemoglobin From Trematomus Bernacchii in the T Quaternary Structure (Fully Ligated State). within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe202 b:40.0 occ:1.00 FE C:HEM202 0.0 40.0 1.0 N C:NO201 1.8 52.4 1.0 ND C:HEM202 2.0 15.6 1.0 NB C:HEM202 2.0 5.1 1.0 NC C:HEM202 2.0 10.2 1.0 NA C:HEM202 2.0 14.7 1.0 NE2 C:HIS88 2.1 55.6 1.0 CE1 C:HIS88 2.7 58.6 1.0 O C:NO201 3.0 33.8 1.0 C4D C:HEM202 3.0 20.6 1.0 C1D C:HEM202 3.0 17.1 1.0 C4B C:HEM202 3.0 15.0 1.0 C1B C:HEM202 3.0 13.4 1.0 C4A C:HEM202 3.1 18.8 1.0 C4C C:HEM202 3.1 4.5 1.0 C1C C:HEM202 3.1 14.6 1.0 C1A C:HEM202 3.1 18.0 1.0 CD2 C:HIS88 3.4 49.9 1.0 CHA C:HEM202 3.4 19.7 1.0 CHD C:HEM202 3.4 15.9 1.0 CHB C:HEM202 3.4 19.3 1.0 CHC C:HEM202 3.4 15.3 1.0 ND1 C:HIS88 3.9 55.7 1.0 NE2 C:HIS59 4.1 37.5 1.0 C3D C:HEM202 4.2 15.5 1.0 C2D C:HEM202 4.2 19.2 1.0 C2B C:HEM202 4.3 12.4 1.0 C3B C:HEM202 4.3 16.5 1.0 CG2 C:VAL63 4.3 7.2 1.0 C3C C:HEM202 4.3 11.1 1.0 C3A C:HEM202 4.3 21.4 1.0 C2C C:HEM202 4.3 6.9 1.0 C2A C:HEM202 4.3 21.0 1.0 CG C:HIS88 4.3 51.2 1.0 CE1 C:HIS59 4.8 41.7 1.0

Iron binding site 4 out of 4 in the Crystallographic Analysis of the Interaction of Nitric Oxide with Hemoglobin From Trematomus Bernacchii in the T Quaternary Structure (Fully Ligated State).


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Crystallographic Analysis of the Interaction of Nitric Oxide with Hemoglobin From Trematomus Bernacchii in the T Quaternary Structure (Fully Ligated State). within 5.0Å range: probe atom residue distance (Å) B Occ D:Fe202 b:39.3 occ:1.00 FE D:HEM202 0.0 39.3 1.0 N D:NO201 1.8 96.4 0.7 NC D:HEM202 2.0 33.1 1.0 ND D:HEM202 2.0 29.4 1.0 NB D:HEM202 2.0 21.2 1.0 NA D:HEM202 2.0 36.8 1.0 NE2 D:HIS92 2.1 50.9 1.0 CE1 D:HIS92 2.9 47.0 1.0 O D:NO201 3.0 98.0 0.7 C4D D:HEM202 3.0 35.2 1.0 C4B D:HEM202 3.0 28.3 1.0 C1D D:HEM202 3.0 31.9 1.0 C1C D:HEM202 3.0 35.2 1.0 C4C D:HEM202 3.1 29.4 1.0 C1A D:HEM202 3.1 40.4 1.0 C4A D:HEM202 3.1 33.1 1.0 C1B D:HEM202 3.1 27.2 1.0 CD2 D:HIS92 3.2 47.2 1.0 CHA D:HEM202 3.4 39.8 1.0 CHC D:HEM202 3.4 31.9 1.0 CHD D:HEM202 3.4 30.6 1.0 CHB D:HEM202 3.4 31.4 1.0 CG2 D:VAL67 4.0 23.6 1.0 ND1 D:HIS92 4.1 41.5 1.0 C2D D:HEM202 4.3 35.8 1.0 C3D D:HEM202 4.3 37.0 1.0 CG D:HIS92 4.3 42.5 1.0 C2C D:HEM202 4.3 31.7 1.0 C3C D:HEM202 4.3 27.5 1.0 C3B D:HEM202 4.3 22.6 1.0 C3A D:HEM202 4.3 33.1 1.0 C2B D:HEM202 4.3 26.7 1.0 C2A D:HEM202 4.3 35.4 1.0 NE2 D:HIS63 4.8 38.1 1.0

A.Merlino, M.R.Fuchs, A.Pica, A.Balsamo, F.S.Dworkowski, G.Pompidor, L.Mazzarella, A.Vergara. Selective X-Ray-Induced No Photodissociation in Haemoglobin Crystals: Evidence From A Raman-Assisted Crystallographic Study. Acta Crystallogr.,Sect.D V. 69 137 2013.
ISSN: ISSN 0907-4449
PubMed: 23275172
DOI: 10.1107/S0907444912042229