Iron in PDB 1rqa: Crystallographic Analysis of the Interaction of Nitric Oxide with Quaternary-T Human Hemoglobin. Beta W73E Hemoglobin Exposed to No Under Anaerobic Conditions

The structure of Crystallographic Analysis of the Interaction of Nitric Oxide with Quaternary-T Human Hemoglobin. Beta W73E Hemoglobin Exposed to No Under Anaerobic Conditions, PDB code: 1rqa was solved by N.-L.Chan, J.S.Kavanaugh, P.H.Rogers, A.Arnone, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	10.00 / 2.11
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	95.300, 97.800, 66.800, 90.00, 90.00, 90.00
R / Rfree (%)	18.8 / 23.1

The binding sites of Iron atom in the Crystallographic Analysis of the Interaction of Nitric Oxide with Quaternary-T Human Hemoglobin. Beta W73E Hemoglobin Exposed to No Under Anaerobic Conditions (pdb code 1rqa). 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 Quaternary-T Human Hemoglobin. Beta W73E Hemoglobin Exposed to No Under Anaerobic Conditions, PDB code: 1rqa:
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 Quaternary-T Human Hemoglobin. Beta W73E Hemoglobin Exposed to No Under Anaerobic Conditions


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 Quaternary-T Human Hemoglobin. Beta W73E Hemoglobin Exposed to No Under Anaerobic Conditions within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe142 b:19.7 occ:1.00 FE A:HEM142 0.0 19.7 1.0 N A:NO150 1.7 21.8 1.0 NC A:HEM142 2.0 21.0 1.0 NA A:HEM142 2.0 21.4 1.0 ND A:HEM142 2.1 21.9 1.0 NB A:HEM142 2.1 20.4 1.0 NE2 A:HIS87 2.3 21.3 1.0 O A:NO150 2.7 23.1 1.0 C1C A:HEM142 3.0 15.8 1.0 C4D A:HEM142 3.1 22.0 1.0 C1D A:HEM142 3.1 19.1 1.0 C4B A:HEM142 3.1 17.9 1.0 C1A A:HEM142 3.1 23.2 1.0 C1B A:HEM142 3.1 21.0 1.0 C4C A:HEM142 3.1 16.1 1.0 C4A A:HEM142 3.1 21.0 1.0 CE1 A:HIS87 3.1 22.2 1.0 CD2 A:HIS87 3.4 22.9 1.0 CHC A:HEM142 3.6 19.7 1.0 CHD A:HEM142 3.6 19.3 1.0 CHA A:HEM142 3.6 23.5 1.0 CHB A:HEM142 3.6 20.1 1.0 C2C A:HEM142 4.2 18.4 1.0 C2A A:HEM142 4.2 24.2 1.0 C3C A:HEM142 4.2 17.6 1.0 C3A A:HEM142 4.2 22.5 1.0 ND1 A:HIS87 4.3 20.8 1.0 NE2 A:HIS58 4.3 24.5 1.0 C3B A:HEM142 4.3 18.8 1.0 C3D A:HEM142 4.3 22.3 1.0 C2D A:HEM142 4.3 20.3 1.0 C2B A:HEM142 4.3 19.4 1.0 CG A:HIS87 4.4 23.0 1.0 CG2 A:VAL62 4.8 19.1 1.0 CE1 A:HIS58 5.0 25.3 1.0

Iron binding site 2 out of 4 in the Crystallographic Analysis of the Interaction of Nitric Oxide with Quaternary-T Human Hemoglobin. Beta W73E Hemoglobin Exposed to No Under Anaerobic Conditions


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 Quaternary-T Human Hemoglobin. Beta W73E Hemoglobin Exposed to No Under Anaerobic Conditions within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe147 b:13.5 occ:1.00 FE B:HEM147 0.0 13.5 1.0 N B:NO150 1.8 15.2 1.0 NA B:HEM147 1.9 15.3 1.0 NC B:HEM147 2.0 13.7 1.0 NB B:HEM147 2.1 13.6 1.0 ND B:HEM147 2.1 13.8 1.0 NE2 B:HIS92 2.2 11.3 1.0 O B:NO150 2.5 15.7 1.0 C1A B:HEM147 3.0 11.3 1.0 C4C B:HEM147 3.0 11.7 1.0 C1D B:HEM147 3.0 14.6 1.0 C4A B:HEM147 3.0 13.4 1.0 C4B B:HEM147 3.0 11.3 1.0 C1C B:HEM147 3.0 9.6 1.0 C1B B:HEM147 3.1 12.9 1.0 C4D B:HEM147 3.1 12.5 1.0 CE1 B:HIS92 3.1 9.7 1.0 CD2 B:HIS92 3.3 12.2 1.0 CHD B:HEM147 3.5 11.7 1.0 CHC B:HEM147 3.6 10.2 1.0 CHA B:HEM147 3.6 8.2 1.0 CHB B:HEM147 3.6 15.9 1.0 C2A B:HEM147 4.1 13.8 1.0 C3A B:HEM147 4.1 14.4 1.0 C3C B:HEM147 4.1 12.9 1.0 C2C B:HEM147 4.1 13.6 1.0 ND1 B:HIS92 4.3 10.4 1.0 C3B B:HEM147 4.3 13.1 1.0 NE2 B:HIS63 4.3 15.7 1.0 C2D B:HEM147 4.3 12.9 1.0 C2B B:HEM147 4.3 9.7 1.0 C3D B:HEM147 4.4 14.2 1.0 CG B:HIS92 4.4 13.0 1.0 CG2 B:VAL67 4.4 16.6 1.0

Iron binding site 3 out of 4 in the Crystallographic Analysis of the Interaction of Nitric Oxide with Quaternary-T Human Hemoglobin. Beta W73E Hemoglobin Exposed to No Under Anaerobic Conditions


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 Quaternary-T Human Hemoglobin. Beta W73E Hemoglobin Exposed to No Under Anaerobic Conditions within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe142 b:19.2 occ:1.00 FE C:HEM142 0.0 19.2 1.0 N C:NO150 1.7 20.0 1.0 NC C:HEM142 2.0 18.9 1.0 NA C:HEM142 2.0 20.1 1.0 NB C:HEM142 2.1 18.6 1.0 ND C:HEM142 2.1 20.1 1.0 NE2 C:HIS87 2.2 21.7 1.0 O C:NO150 2.6 21.2 1.0 C1B C:HEM142 3.0 19.1 1.0 C4B C:HEM142 3.0 17.8 1.0 C4C C:HEM142 3.0 15.3 1.0 C4A C:HEM142 3.0 18.8 1.0 CE1 C:HIS87 3.1 25.6 1.0 C1C C:HEM142 3.1 14.0 1.0 C1D C:HEM142 3.1 17.1 1.0 C1A C:HEM142 3.1 18.3 1.0 C4D C:HEM142 3.1 16.8 1.0 CD2 C:HIS87 3.3 22.0 1.0 CHD C:HEM142 3.5 16.0 1.0 CHB C:HEM142 3.5 16.2 1.0 CHC C:HEM142 3.6 16.7 1.0 CHA C:HEM142 3.6 17.9 1.0 C2C C:HEM142 4.2 17.1 1.0 C3C C:HEM142 4.2 14.8 1.0 C3A C:HEM142 4.2 22.2 1.0 C2A C:HEM142 4.2 22.4 1.0 ND1 C:HIS87 4.2 23.9 1.0 C3B C:HEM142 4.3 18.0 1.0 C2B C:HEM142 4.3 16.9 1.0 C3D C:HEM142 4.4 18.4 1.0 C2D C:HEM142 4.4 18.0 1.0 CG C:HIS87 4.4 22.7 1.0 NE2 C:HIS58 4.5 23.2 1.0 CG2 C:VAL62 4.9 21.0 1.0

Iron binding site 4 out of 4 in the Crystallographic Analysis of the Interaction of Nitric Oxide with Quaternary-T Human Hemoglobin. Beta W73E Hemoglobin Exposed to No Under Anaerobic Conditions


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 Quaternary-T Human Hemoglobin. Beta W73E Hemoglobin Exposed to No Under Anaerobic Conditions within 5.0Å range: probe atom residue distance (Å) B Occ D:Fe147 b:20.4 occ:1.00 FE D:HEM147 0.0 20.4 1.0 N D:NO150 1.8 21.4 1.0 NC D:HEM147 2.0 20.2 1.0 NA D:HEM147 2.0 20.9 1.0 ND D:HEM147 2.1 20.2 1.0 NB D:HEM147 2.1 21.0 1.0 NE2 D:HIS92 2.2 17.1 1.0 O D:NO150 2.7 22.2 1.0 C1C D:HEM147 3.0 15.3 1.0 C1D D:HEM147 3.0 21.3 1.0 C1A D:HEM147 3.0 21.4 1.0 C4C D:HEM147 3.0 18.9 1.0 C4B D:HEM147 3.1 18.6 1.0 C4D D:HEM147 3.1 21.7 1.0 CE1 D:HIS92 3.1 17.9 1.0 C4A D:HEM147 3.1 19.6 1.0 C1B D:HEM147 3.1 21.8 1.0 CD2 D:HIS92 3.2 19.0 1.0 CHC D:HEM147 3.5 16.7 1.0 CHA D:HEM147 3.6 20.9 1.0 CHD D:HEM147 3.6 19.4 1.0 CHB D:HEM147 3.6 22.2 1.0 C2C D:HEM147 4.1 16.6 1.0 C3C D:HEM147 4.2 18.8 1.0 C2A D:HEM147 4.2 23.4 1.0 C3A D:HEM147 4.2 20.5 1.0 ND1 D:HIS92 4.2 23.5 1.0 C3B D:HEM147 4.3 18.7 1.0 C3D D:HEM147 4.3 23.6 1.0 C2D D:HEM147 4.3 22.3 1.0 CG D:HIS92 4.3 20.0 1.0 C2B D:HEM147 4.4 21.9 1.0 NE2 D:HIS63 4.5 24.4 1.0 CG2 D:VAL67 4.6 22.7 1.0

N.-L.Chan, J.S.Kavanaugh, P.H.Rogers, A.Arnone. Crystallographic Analysis of the Interaction of Nitric Oxide with Quaternary-T Human Hemoglobin. Biochemistry V. 43 118 2004.
ISSN: ISSN 0006-2960
PubMed: 14705937
DOI: 10.1021/BI0497603