Iron in PDB 2w72: Deoxygenated Structure of A Distal Site Hemoglobin Mutant Plus Xe

The structure of Deoxygenated Structure of A Distal Site Hemoglobin Mutant Plus Xe, PDB code: 2w72 was solved by A.E.Miele, F.Draghi, G.Sciara, K.A.Johnson, F.Renzi, B.Vallone, M.Brunori, C.Savino, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	17.32 / 1.07
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	61.957, 82.447, 53.531, 90.00, 99.60, 90.00
R / Rfree (%)	12.9 / 15.3

The structure of Deoxygenated Structure of A Distal Site Hemoglobin Mutant Plus Xe also contains other interesting chemical elements:

Potassium	(K)	3 atoms
Xenon	(Xe)	23 atoms

The binding sites of Iron atom in the Deoxygenated Structure of A Distal Site Hemoglobin Mutant Plus Xe (pdb code 2w72). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 4 binding sites of Iron where determined in the Deoxygenated Structure of A Distal Site Hemoglobin Mutant Plus Xe, PDB code: 2w72:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in the Deoxygenated Structure of A Distal Site Hemoglobin Mutant Plus Xe


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Deoxygenated Structure of A Distal Site Hemoglobin Mutant Plus Xe within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe1142 b:7.4 occ:1.00 FE A:HEM1142 0.0 7.4 1.0 ND A:HEM1142 2.1 7.7 1.0 NB A:HEM1142 2.1 7.6 1.0 NC A:HEM1142 2.1 7.3 1.0 NA A:HEM1142 2.1 8.4 1.0 NE2 A:HIS87 2.2 7.3 1.0 CE1 A:HIS87 3.0 7.4 1.0 C1B A:HEM1142 3.1 8.5 1.0 C1D A:HEM1142 3.1 8.0 1.0 C4B A:HEM1142 3.1 7.8 1.0 C1C A:HEM1142 3.1 7.4 1.0 C4A A:HEM1142 3.1 8.6 1.0 C4C A:HEM1142 3.1 7.3 1.0 C4D A:HEM1142 3.1 8.2 1.0 C1A A:HEM1142 3.1 8.6 1.0 CD2 A:HIS87 3.3 7.7 1.0 CHB A:HEM1142 3.4 8.6 1.0 CHD A:HEM1142 3.4 7.8 1.0 CHC A:HEM1142 3.5 7.6 1.0 CHA A:HEM1142 3.5 9.0 1.0 NE2 A:GLN58 3.9 11.4 1.0 OH A:TYR29 3.9 10.8 1.0 ND1 A:HIS87 4.2 7.8 1.0 C2D A:HEM1142 4.3 8.8 1.0 C3B A:HEM1142 4.3 8.0 1.0 C2B A:HEM1142 4.3 8.9 1.0 C3D A:HEM1142 4.3 9.5 1.0 C2C A:HEM1142 4.3 7.5 1.0 C3C A:HEM1142 4.3 7.7 1.0 C3A A:HEM1142 4.3 9.3 1.0 C2A A:HEM1142 4.4 9.2 1.0 CG A:HIS87 4.4 7.2 1.0 CD1 A:LEU91 4.4 9.0 1.0 CG2 A:VAL62 4.7 11.9 1.0

Iron binding site 2 out of 4 in the Deoxygenated Structure of A Distal Site Hemoglobin Mutant Plus Xe


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Deoxygenated Structure of A Distal Site Hemoglobin Mutant Plus Xe within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe1147 b:7.9 occ:1.00 FE B:HEM1147 0.0 7.9 1.0 NA B:HEM1147 2.0 8.2 1.0 ND B:HEM1147 2.1 8.0 1.0 NB B:HEM1147 2.1 8.2 1.0 NC B:HEM1147 2.1 7.7 1.0 NE2 B:HIS92 2.1 7.7 1.0 CE1 B:HIS92 3.1 7.7 1.0 C1D B:HEM1147 3.1 7.8 1.0 C4A B:HEM1147 3.1 8.7 1.0 C1B B:HEM1147 3.1 8.3 1.0 C4D B:HEM1147 3.1 8.9 1.0 C1A B:HEM1147 3.1 9.0 1.0 C4B B:HEM1147 3.1 7.7 1.0 C4C B:HEM1147 3.1 7.5 1.0 C1C B:HEM1147 3.1 7.6 1.0 CD2 B:HIS92 3.2 8.0 1.0 CHD B:HEM1147 3.4 8.4 1.0 CHB B:HEM1147 3.4 9.0 1.0 CHA B:HEM1147 3.4 9.4 1.0 CHC B:HEM1147 3.5 7.9 1.0 CG2 B:VAL67 4.1 9.9 1.0 NE2 B:GLN63 4.1 12.9 1.0 ND1 B:HIS92 4.2 8.4 1.0 C2B B:HEM1147 4.3 8.7 1.0 C2D B:HEM1147 4.3 9.2 1.0 C3B B:HEM1147 4.3 9.6 1.0 C3A B:HEM1147 4.3 10.1 1.0 C2A B:HEM1147 4.3 9.8 1.0 C3C B:HEM1147 4.3 7.4 1.0 C3D B:HEM1147 4.3 9.0 1.0 C2C B:HEM1147 4.3 8.0 1.0 CG B:HIS92 4.3 7.8 1.0 OH B:TYR28 4.7 15.7 1.0 CD1 B:LEU96 4.8 10.2 1.0

Iron binding site 3 out of 4 in the Deoxygenated Structure of A Distal Site Hemoglobin Mutant Plus Xe


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Deoxygenated Structure of A Distal Site Hemoglobin Mutant Plus Xe within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe1142 b:8.3 occ:1.00 FE C:HEM1142 0.0 8.3 1.0 NB C:HEM1142 2.1 8.5 1.0 NA C:HEM1142 2.1 9.2 1.0 ND C:HEM1142 2.1 8.8 1.0 NC C:HEM1142 2.1 7.9 1.0 CE1 C:HIS87 2.2 9.3 0.8 NE2 C:HIS87 2.2 4.4 0.2 NE2 C:HIS87 3.0 13.6 0.8 C1D C:HEM1142 3.1 8.3 1.0 C1B C:HEM1142 3.1 9.1 1.0 C4B C:HEM1142 3.1 8.6 1.0 C4A C:HEM1142 3.1 10.1 1.0 C1C C:HEM1142 3.1 8.3 1.0 C4C C:HEM1142 3.1 7.6 1.0 C1A C:HEM1142 3.1 9.6 1.0 C4D C:HEM1142 3.1 8.8 1.0 CE1 C:HIS87 3.2 4.6 0.2 CD2 C:HIS87 3.3 3.7 0.2 ND1 C:HIS87 3.4 12.3 0.8 CHB C:HEM1142 3.4 9.7 1.0 CHC C:HEM1142 3.4 9.1 1.0 CHD C:HEM1142 3.4 9.0 1.0 CHA C:HEM1142 3.5 9.9 1.0 OH C:TYR29 3.9 10.3 1.0 NE2 C:GLN58 3.9 11.0 1.0 CD2 C:HIS87 4.2 9.6 0.8 C3B C:HEM1142 4.3 9.9 1.0 C2D C:HEM1142 4.3 9.0 1.0 ND1 C:HIS87 4.3 5.0 0.2 C3A C:HEM1142 4.3 11.2 1.0 C2B C:HEM1142 4.3 9.7 1.0 C2C C:HEM1142 4.3 8.1 1.0 C2A C:HEM1142 4.3 10.9 1.0 C3C C:HEM1142 4.3 8.1 1.0 C3D C:HEM1142 4.4 9.5 1.0 CG C:HIS87 4.4 5.6 0.2 CG C:HIS87 4.4 9.6 0.8 CD1 C:LEU91 4.4 11.1 1.0 CG2 C:VAL62 4.9 11.9 1.0

Iron binding site 4 out of 4 in the Deoxygenated Structure of A Distal Site Hemoglobin Mutant Plus Xe


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Deoxygenated Structure of A Distal Site Hemoglobin Mutant Plus Xe within 5.0Å range: probe atom residue distance (Å) B Occ D:Fe1147 b:7.2 occ:1.00 FE D:HEM1147 0.0 7.2 1.0 NA D:HEM1147 2.1 7.7 1.0 ND D:HEM1147 2.1 7.3 1.0 NB D:HEM1147 2.1 7.2 1.0 NC D:HEM1147 2.1 7.1 1.0 NE2 D:HIS92 2.1 7.5 1.0 CE1 D:HIS92 3.1 8.4 1.0 C1B D:HEM1147 3.1 7.4 1.0 C4A D:HEM1147 3.1 7.7 1.0 C1D D:HEM1147 3.1 7.5 1.0 C4D D:HEM1147 3.1 7.6 1.0 C1A D:HEM1147 3.1 7.8 1.0 C1C D:HEM1147 3.1 7.5 1.0 C4C D:HEM1147 3.1 7.6 1.0 C4B D:HEM1147 3.1 7.3 1.0 CD2 D:HIS92 3.2 7.6 1.0 CHB D:HEM1147 3.4 7.9 1.0 CHD D:HEM1147 3.4 7.8 1.0 CHC D:HEM1147 3.4 8.0 1.0 CHA D:HEM1147 3.4 8.4 1.0 CG2 D:VAL67 4.0 8.9 1.0 NE2 D:GLN63 4.1 9.3 1.0 ND1 D:HIS92 4.2 8.2 1.0 C3B D:HEM1147 4.3 7.9 1.0 C2D D:HEM1147 4.3 8.0 1.0 C2B D:HEM1147 4.3 7.7 1.0 C3C D:HEM1147 4.3 7.8 1.0 C3A D:HEM1147 4.3 8.8 1.0 C2C D:HEM1147 4.3 8.1 1.0 C2A D:HEM1147 4.3 9.0 1.0 C3D D:HEM1147 4.3 7.9 1.0 CG D:HIS92 4.3 7.5 1.0 CD1 D:LEU96 4.8 9.9 1.0 OH D:TYR28 5.0 11.2 1.0

C.Savino, A.E.Miele, F.Draghi, K.A.Johnson, G.Sciara, M.Brunori, B.Vallone. Pattern of Cavities in Globins: the Case of Human Hemoglobin. Biopolymers V. 91 1097 2009.
ISSN: ISSN 0006-3525
PubMed: 19365817
DOI: 10.1002/BIP.21201