Iron in PDB 1f5p: 2.9 Angstrom Crystal Structure of Lamprey Hemoglobin That Has Been Exposed to Carbon Monoxide.

The structure of 2.9 Angstrom Crystal Structure of Lamprey Hemoglobin That Has Been Exposed to Carbon Monoxide., PDB code: 1f5p was solved by H.A.Heaslet, W.E.Royer Jr., with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	10.00 / 2.90
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	82.500, 96.200, 145.100, 90.00, 90.00, 90.00
R / Rfree (%)	20.6 / 25.6

The binding sites of Iron atom in the 2.9 Angstrom Crystal Structure of Lamprey Hemoglobin That Has Been Exposed to Carbon Monoxide. (pdb code 1f5p). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 6 binding sites of Iron where determined in the 2.9 Angstrom Crystal Structure of Lamprey Hemoglobin That Has Been Exposed to Carbon Monoxide., PDB code: 1f5p:
Jump to Iron binding site number: 1; 2; 3; 4; 5; 6;

Iron binding site 1 out of 6 in the 2.9 Angstrom Crystal Structure of Lamprey Hemoglobin That Has Been Exposed to Carbon Monoxide.


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of 2.9 Angstrom Crystal Structure of Lamprey Hemoglobin That Has Been Exposed to Carbon Monoxide. within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe150 b:59.3 occ:1.00 FE A:HEM150 0.0 59.3 1.0 C A:CMO151 1.9 33.9 1.0 NE2 A:HIS105 1.9 35.0 1.0 NC A:HEM150 2.0 59.3 1.0 NA A:HEM150 2.0 59.3 1.0 ND A:HEM150 2.0 59.3 1.0 NB A:HEM150 2.0 59.3 1.0 CE1 A:HIS105 2.8 35.0 1.0 C1A A:HEM150 3.0 59.3 1.0 C4C A:HEM150 3.0 59.3 1.0 C4D A:HEM150 3.0 59.3 1.0 C1C A:HEM150 3.0 59.3 1.0 C4A A:HEM150 3.1 59.3 1.0 C1D A:HEM150 3.1 59.3 1.0 O A:CMO151 3.1 33.9 1.0 CD2 A:HIS105 3.1 35.0 1.0 C1B A:HEM150 3.1 59.3 1.0 C4B A:HEM150 3.1 59.3 1.0 CHA A:HEM150 3.4 59.3 1.0 CHD A:HEM150 3.4 59.3 1.0 CHC A:HEM150 3.5 59.3 1.0 CHB A:HEM150 3.5 59.3 1.0 ND1 A:HIS105 4.0 35.0 1.0 CG A:HIS105 4.2 35.0 1.0 C3C A:HEM150 4.3 59.3 1.0 C2A A:HEM150 4.3 59.3 1.0 C2C A:HEM150 4.3 59.3 1.0 C3A A:HEM150 4.3 59.3 1.0 C3D A:HEM150 4.3 59.3 1.0 C2D A:HEM150 4.3 59.3 1.0 C2B A:HEM150 4.3 59.3 1.0 C3B A:HEM150 4.4 59.3 1.0 NE2 A:HIS73 4.8 60.0 1.0

Iron binding site 2 out of 6 in the 2.9 Angstrom Crystal Structure of Lamprey Hemoglobin That Has Been Exposed to Carbon Monoxide.


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of 2.9 Angstrom Crystal Structure of Lamprey Hemoglobin That Has Been Exposed to Carbon Monoxide. within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe150 b:57.6 occ:1.00 FE B:HEM150 0.0 57.6 1.0 C B:CMO151 1.9 32.2 1.0 ND B:HEM150 1.9 57.6 1.0 NA B:HEM150 2.0 57.6 1.0 NE2 B:HIS105 2.0 46.0 1.0 NC B:HEM150 2.0 57.6 1.0 NB B:HEM150 2.1 57.6 1.0 CE1 B:HIS105 2.9 46.0 1.0 C4D B:HEM150 3.0 57.6 1.0 C1A B:HEM150 3.0 57.6 1.0 C1D B:HEM150 3.0 57.6 1.0 C1C B:HEM150 3.0 57.6 1.0 O B:CMO151 3.0 32.2 1.0 C4C B:HEM150 3.1 57.6 1.0 C4A B:HEM150 3.1 57.6 1.0 CD2 B:HIS105 3.1 46.0 1.0 C4B B:HEM150 3.1 57.6 1.0 C1B B:HEM150 3.1 57.6 1.0 CHA B:HEM150 3.3 57.6 1.0 CHD B:HEM150 3.4 57.6 1.0 CHC B:HEM150 3.4 57.6 1.0 CHB B:HEM150 3.5 57.6 1.0 ND1 B:HIS105 4.1 46.0 1.0 CG B:HIS105 4.2 46.0 1.0 C2D B:HEM150 4.2 57.6 1.0 C3D B:HEM150 4.2 57.6 1.0 C2A B:HEM150 4.2 57.6 1.0 C2C B:HEM150 4.3 57.6 1.0 C3A B:HEM150 4.3 57.6 1.0 C3C B:HEM150 4.3 57.6 1.0 C3B B:HEM150 4.4 57.6 1.0 C2B B:HEM150 4.4 57.6 1.0 NE2 B:HIS73 4.5 45.4 1.0

Iron binding site 3 out of 6 in the 2.9 Angstrom Crystal Structure of Lamprey Hemoglobin That Has Been Exposed to Carbon Monoxide.


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of 2.9 Angstrom Crystal Structure of Lamprey Hemoglobin That Has Been Exposed to Carbon Monoxide. within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe150 b:52.0 occ:1.00 FE C:HEM150 0.0 52.0 1.0 C C:CMO151 1.9 26.6 1.0 NC C:HEM150 2.0 52.0 1.0 NB C:HEM150 2.0 52.0 1.0 ND C:HEM150 2.0 52.0 1.0 NA C:HEM150 2.0 52.0 1.0 NE2 C:HIS105 2.1 57.1 1.0 CE1 C:HIS105 3.0 57.1 1.0 C1C C:HEM150 3.0 52.0 1.0 C4B C:HEM150 3.1 52.0 1.0 C4C C:HEM150 3.1 52.0 1.0 C1B C:HEM150 3.1 52.0 1.0 C4D C:HEM150 3.1 52.0 1.0 C4A C:HEM150 3.1 52.0 1.0 C1D C:HEM150 3.1 52.0 1.0 C1A C:HEM150 3.1 52.0 1.0 O C:CMO151 3.1 26.6 1.0 CD2 C:HIS105 3.2 57.1 1.0 CHC C:HEM150 3.4 52.0 1.0 CHD C:HEM150 3.5 52.0 1.0 CHA C:HEM150 3.5 52.0 1.0 CHB C:HEM150 3.5 52.0 1.0 ND1 C:HIS105 4.2 57.1 1.0 C2C C:HEM150 4.3 52.0 1.0 C2B C:HEM150 4.3 52.0 1.0 C3B C:HEM150 4.3 52.0 1.0 CG C:HIS105 4.3 57.1 1.0 NE2 C:HIS73 4.3 55.1 0.5 C3C C:HEM150 4.3 52.0 1.0 C3D C:HEM150 4.3 52.0 1.0 C3A C:HEM150 4.3 52.0 1.0 C2A C:HEM150 4.3 52.0 1.0 C2D C:HEM150 4.4 52.0 1.0

Iron binding site 4 out of 6 in the 2.9 Angstrom Crystal Structure of Lamprey Hemoglobin That Has Been Exposed to Carbon Monoxide.


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of 2.9 Angstrom Crystal Structure of Lamprey Hemoglobin That Has Been Exposed to Carbon Monoxide. within 5.0Å range: probe atom residue distance (Å) B Occ D:Fe150 b:42.9 occ:1.00 FE D:HEM150 0.0 42.9 1.0 ND D:HEM150 1.9 42.9 1.0 C D:CMO151 1.9 17.5 1.0 NC D:HEM150 2.0 42.9 1.0 NA D:HEM150 2.0 42.9 1.0 NB D:HEM150 2.1 42.9 1.0 NE2 D:HIS105 2.1 53.8 1.0 C4D D:HEM150 2.9 42.9 1.0 C1D D:HEM150 3.0 42.9 1.0 C1A D:HEM150 3.0 42.9 1.0 C1C D:HEM150 3.0 42.9 1.0 C4C D:HEM150 3.0 42.9 1.0 CE1 D:HIS105 3.1 53.8 1.0 C4A D:HEM150 3.1 42.9 1.0 C4B D:HEM150 3.1 42.9 1.0 C1B D:HEM150 3.2 42.9 1.0 O D:CMO151 3.2 17.5 1.0 CD2 D:HIS105 3.2 53.8 1.0 CHA D:HEM150 3.3 42.9 1.0 CHD D:HEM150 3.4 42.9 1.0 CHC D:HEM150 3.4 42.9 1.0 CHB D:HEM150 3.5 42.9 1.0 C3D D:HEM150 4.2 42.9 1.0 C2D D:HEM150 4.2 42.9 1.0 C2C D:HEM150 4.2 42.9 1.0 C2A D:HEM150 4.2 42.9 1.0 ND1 D:HIS105 4.3 53.8 1.0 C3C D:HEM150 4.3 42.9 1.0 C3A D:HEM150 4.3 42.9 1.0 C3B D:HEM150 4.3 42.9 1.0 CG D:HIS105 4.3 53.8 1.0 C2B D:HEM150 4.4 42.9 1.0 NE2 D:HIS73 4.4 41.5 1.0

Iron binding site 5 out of 6 in the 2.9 Angstrom Crystal Structure of Lamprey Hemoglobin That Has Been Exposed to Carbon Monoxide.


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 5 of 2.9 Angstrom Crystal Structure of Lamprey Hemoglobin That Has Been Exposed to Carbon Monoxide. within 5.0Å range: probe atom residue distance (Å) B Occ E:Fe150 b:43.8 occ:1.00 FE E:HEM150 0.0 43.8 1.0 C E:CMO151 1.9 18.4 1.0 ND E:HEM150 2.0 43.8 1.0 NA E:HEM150 2.0 43.8 1.0 NC E:HEM150 2.0 43.8 1.0 NB E:HEM150 2.0 43.8 1.0 NE2 E:HIS105 2.1 35.0 1.0 C4D E:HEM150 3.0 43.8 1.0 C1A E:HEM150 3.0 43.8 1.0 CE1 E:HIS105 3.0 35.0 1.0 C1D E:HEM150 3.0 43.8 1.0 C4B E:HEM150 3.1 43.8 1.0 C1B E:HEM150 3.1 43.8 1.0 C1C E:HEM150 3.1 43.8 1.0 C4C E:HEM150 3.1 43.8 1.0 O E:CMO151 3.1 18.4 1.0 C4A E:HEM150 3.1 43.8 1.0 CD2 E:HIS105 3.2 35.0 1.0 CHA E:HEM150 3.4 43.8 1.0 CHC E:HEM150 3.5 43.8 1.0 CHD E:HEM150 3.5 43.8 1.0 CHB E:HEM150 3.5 43.8 1.0 ND1 E:HIS105 4.2 35.0 1.0 C3D E:HEM150 4.2 43.8 1.0 C2D E:HEM150 4.2 43.8 1.0 C2A E:HEM150 4.3 43.8 1.0 C2C E:HEM150 4.3 43.8 1.0 C2B E:HEM150 4.3 43.8 1.0 CG E:HIS105 4.3 35.0 1.0 C3B E:HEM150 4.3 43.8 1.0 C3C E:HEM150 4.3 43.8 1.0 C3A E:HEM150 4.3 43.8 1.0 NE2 E:HIS73 4.4 47.5 1.0

Iron binding site 6 out of 6 in the 2.9 Angstrom Crystal Structure of Lamprey Hemoglobin That Has Been Exposed to Carbon Monoxide.


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 6 of 2.9 Angstrom Crystal Structure of Lamprey Hemoglobin That Has Been Exposed to Carbon Monoxide. within 5.0Å range: probe atom residue distance (Å) B Occ F:Fe150 b:44.6 occ:1.00 FE F:HEM150 0.0 44.6 1.0 C F:CMO151 1.9 19.2 1.0 NA F:HEM150 1.9 44.6 1.0 NC F:HEM150 2.0 44.6 1.0 NB F:HEM150 2.0 44.6 1.0 ND F:HEM150 2.0 44.6 1.0 NE2 F:HIS105 2.1 47.5 1.0 CE1 F:HIS105 3.0 47.5 1.0 C1A F:HEM150 3.0 44.6 1.0 C4A F:HEM150 3.0 44.6 1.0 C1D F:HEM150 3.0 44.6 1.0 C1B F:HEM150 3.0 44.6 1.0 C4D F:HEM150 3.0 44.6 1.0 C4C F:HEM150 3.0 44.6 1.0 C1C F:HEM150 3.0 44.6 1.0 C4B F:HEM150 3.0 44.6 1.0 O F:CMO151 3.1 19.2 1.0 CD2 F:HIS105 3.3 47.5 1.0 CHD F:HEM150 3.4 44.6 1.0 CHB F:HEM150 3.4 44.6 1.0 CHA F:HEM150 3.4 44.6 1.0 CHC F:HEM150 3.4 44.6 1.0 ND1 F:HIS105 4.2 47.5 1.0 C2A F:HEM150 4.2 44.6 1.0 C3D F:HEM150 4.2 44.6 1.0 C2D F:HEM150 4.2 44.6 1.0 C2B F:HEM150 4.2 44.6 1.0 C3A F:HEM150 4.3 44.6 1.0 C2C F:HEM150 4.3 44.6 1.0 C3C F:HEM150 4.3 44.6 1.0 C3B F:HEM150 4.3 44.6 1.0 CG F:HIS105 4.3 47.5 1.0 NE2 F:HIS73 5.0 15.8 0.5

H.A.Heaslet, W.E.Royer Jr.. Crystalline Ligand Transitions in Lamprey Hemoglobin. Structural Evidence For the Regulation of Oxygen Affinity. J.Biol.Chem. V. 276 26230 2001.
ISSN: ISSN 0021-9258
PubMed: 11340069
DOI: 10.1074/JBC.M101391200