Iron in PDB 1nwn: Crystals of Co-Hbi in Which the Structure Was Converted to Its Unligated State, and Then Converted Back to Its Original Co-Ligated State.

The structure of Crystals of Co-Hbi in Which the Structure Was Converted to Its Unligated State, and Then Converted Back to Its Original Co-Ligated State., PDB code: 1nwn was solved by J.E.Knapp, W.E.Royer Jr., with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	37.79 / 2.80
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	92.620, 43.510, 83.110, 90.00, 121.88, 90.00
R / Rfree (%)	22.2 / 24.8

The binding sites of Iron atom in the Crystals of Co-Hbi in Which the Structure Was Converted to Its Unligated State, and Then Converted Back to Its Original Co-Ligated State. (pdb code 1nwn). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Crystals of Co-Hbi in Which the Structure Was Converted to Its Unligated State, and Then Converted Back to Its Original Co-Ligated State., PDB code: 1nwn:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Crystals of Co-Hbi in Which the Structure Was Converted to Its Unligated State, and Then Converted Back to Its Original Co-Ligated State.


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Crystals of Co-Hbi in Which the Structure Was Converted to Its Unligated State, and Then Converted Back to Its Original Co-Ligated State. within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe147 b:46.6 occ:1.00 FE A:HEM147 0.0 46.6 1.0 C A:CMO148 1.9 46.4 1.0 NB A:HEM147 2.0 46.6 1.0 ND A:HEM147 2.0 46.6 1.0 NA A:HEM147 2.0 46.6 1.0 NC A:HEM147 2.0 46.6 1.0 NE2 A:HIS101 2.0 41.7 1.0 C1B A:HEM147 3.1 46.6 1.0 C1A A:HEM147 3.1 46.6 1.0 CE1 A:HIS101 3.1 41.7 1.0 C1D A:HEM147 3.1 46.6 1.0 CD2 A:HIS101 3.1 41.7 1.0 C4B A:HEM147 3.1 46.6 1.0 C1C A:HEM147 3.1 46.6 1.0 C4C A:HEM147 3.1 46.6 1.0 C4A A:HEM147 3.1 46.6 1.0 C4D A:HEM147 3.1 46.6 1.0 O A:CMO148 3.1 46.4 1.0 CHD A:HEM147 3.4 46.6 1.0 CHB A:HEM147 3.4 46.6 1.0 CHC A:HEM147 3.4 46.6 1.0 CHA A:HEM147 3.4 46.6 1.0 ND1 A:HIS101 4.2 41.7 1.0 CG A:HIS101 4.2 41.7 1.0 C2A A:HEM147 4.3 46.6 1.0 C2B A:HEM147 4.3 46.6 1.0 C3D A:HEM147 4.3 46.6 1.0 C2D A:HEM147 4.3 46.6 1.0 C2C A:HEM147 4.3 46.6 1.0 C3A A:HEM147 4.3 46.6 1.0 C3B A:HEM147 4.3 46.6 1.0 C3C A:HEM147 4.3 46.6 1.0 CE1 A:HIS69 4.9 45.6 1.0 CD1 A:LEU73 4.9 46.6 1.0 CE1 A:PHE111 4.9 51.2 1.0

Iron binding site 2 out of 2 in the Crystals of Co-Hbi in Which the Structure Was Converted to Its Unligated State, and Then Converted Back to Its Original Co-Ligated State.


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Crystals of Co-Hbi in Which the Structure Was Converted to Its Unligated State, and Then Converted Back to Its Original Co-Ligated State. within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe147 b:46.6 occ:1.00 FE B:HEM147 0.0 46.6 1.0 C B:CMO148 1.8 46.4 1.0 ND B:HEM147 2.0 46.6 1.0 NA B:HEM147 2.0 46.6 1.0 NC B:HEM147 2.0 46.6 1.0 NB B:HEM147 2.0 46.6 1.0 NE2 B:HIS101 2.1 41.7 1.0 O B:CMO148 3.0 46.4 1.0 C1D B:HEM147 3.0 46.6 1.0 C4D B:HEM147 3.0 46.6 1.0 C1A B:HEM147 3.0 46.6 1.0 C4C B:HEM147 3.1 46.6 1.0 C1B B:HEM147 3.1 46.6 1.0 C4A B:HEM147 3.1 46.6 1.0 C1C B:HEM147 3.1 46.6 1.0 CE1 B:HIS101 3.1 41.7 1.0 C4B B:HEM147 3.1 46.6 1.0 CD2 B:HIS101 3.1 41.7 1.0 CHD B:HEM147 3.4 46.6 1.0 CHA B:HEM147 3.4 46.6 1.0 CHB B:HEM147 3.5 46.6 1.0 CHC B:HEM147 3.5 46.6 1.0 ND1 B:HIS101 4.2 41.7 1.0 C3D B:HEM147 4.3 46.6 1.0 C2D B:HEM147 4.3 46.6 1.0 C2A B:HEM147 4.3 46.6 1.0 CG B:HIS101 4.3 41.7 1.0 C3A B:HEM147 4.3 46.6 1.0 C2C B:HEM147 4.3 46.6 1.0 C2B B:HEM147 4.3 46.6 1.0 C3C B:HEM147 4.3 46.6 1.0 C3B B:HEM147 4.3 46.6 1.0 CE1 B:HIS69 4.8 45.6 1.0 CD1 B:LEU73 4.9 46.6 1.0 CE1 B:PHE111 4.9 51.2 1.0 NE2 B:HIS69 4.9 45.6 1.0

J.E.Knapp, W.E.Royer Jr.. Ligand-Linked Structural Transitions in Crystals of A Cooperative Dimeric Hemoglobin. Biochemistry V. 42 4640 2003.
ISSN: ISSN 0006-2960
PubMed: 12705827
DOI: 10.1021/BI027136P