Potassium 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:

Iron	(Fe)	4 atoms
Xenon	(Xe)	23 atoms

The binding sites of Potassium 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 Potassium atom.
In total 3 binding sites of Potassium where determined in the Deoxygenated Structure of A Distal Site Hemoglobin Mutant Plus Xe, PDB code: 2w72:
Jump to Potassium binding site number: 1; 2; 3;

Potassium binding site 1 out of 3 in the Deoxygenated Structure of A Distal Site Hemoglobin Mutant Plus Xe


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K 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:K1153 b:59.6 occ:1.00 O A:HOH2183 2.3 33.0 1.0 O A:HOH2084 2.5 33.0 1.0 O A:HOH2145 2.8 23.8 1.0 O C:HOH2076 2.8 32.8 1.0 O C:HOH2155 3.5 33.6 1.0 CZ2 D:TRP37 3.8 10.9 1.0 O C:HOH2139 3.8 32.7 1.0 CH2 D:TRP37 4.1 11.8 1.0 CD2 D:LEU105 4.2 12.2 1.0 O C:HOH2169 4.5 27.9 1.0 CE1 D:TYR35 4.5 10.9 1.0 O C:HOH2077 4.5 29.0 1.0 CD1 D:TYR35 4.6 9.2 1.0 CG A:PRO95 4.8 14.4 1.0 CE2 D:TRP37 5.0 10.1 1.0 CB A:PRO95 5.0 12.9 1.0 CD A:PRO95 5.0 12.7 1.0

Potassium binding site 2 out of 3 in the Deoxygenated Structure of A Distal Site Hemoglobin Mutant Plus Xe


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K 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:K1150 b:32.7 occ:0.80 O B:HOH2041 2.8 30.5 1.0 O B:ALA62 2.9 11.4 1.0 CG B:LYS66 3.6 15.3 0.5 C B:ALA62 3.6 10.6 1.0 CA B:ALA62 3.6 11.6 1.0 CD B:LYS65 3.7 18.3 0.5 CB B:ALA62 3.7 13.4 1.0 CB B:LYS65 3.9 12.8 0.5 CB B:LYS65 4.0 12.3 0.5 CG B:LYS65 4.0 14.9 0.5 CE B:LYS66 4.0 21.9 0.5 CE B:LYS66 4.0 16.4 0.5 N B:LYS66 4.2 10.3 1.0 CD B:LYS66 4.3 19.1 0.5 CB B:LYS66 4.3 11.9 0.5 O B:HOH2108 4.4 42.9 1.0 O B:HOH2106 4.5 26.7 1.0 CE B:LYS65 4.5 19.9 0.5 CD B:LYS65 4.5 14.8 0.5 CB B:LYS66 4.6 12.4 0.5 O B:HOH2049 4.7 41.1 1.0 CA B:LYS66 4.7 11.7 0.5 CA B:LYS66 4.7 11.4 0.5 C B:LYS65 4.7 10.8 1.0 NZ B:LYS65 4.8 22.8 0.5 CG B:LYS65 4.8 12.0 0.5 N B:GLN63 4.8 10.5 1.0 CA B:LYS65 4.8 11.1 0.5 CA B:LYS65 4.9 10.6 0.5 NZ B:LYS66 4.9 15.4 0.5

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


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K 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:K1146 b:21.7 occ:0.80 O D:HOH2078 2.7 38.7 1.0 O C:HOH2057 3.5 31.3 1.0 ND2 D:ASN108 3.6 20.2 0.7 CB C:HIS103 3.8 7.9 1.0 OD1 D:ASN108 3.8 20.4 0.7 CD2 C:LEU100 3.8 10.5 1.0 CG C:HIS103 3.9 7.2 1.0 CG D:ASN108 3.9 14.9 0.7 O D:HOH2173 3.9 42.0 1.0 O C:HOH2058 4.0 37.3 1.0 CD2 C:HIS103 4.0 8.7 1.0 CZ C:PHE36 4.1 11.6 1.0 ND2 D:ASN108 4.2 13.4 0.3 O C:LYS99 4.3 8.7 1.0 ND1 C:HIS103 4.5 8.7 1.0 O C:HOH2153 4.6 14.4 1.0 CA C:LEU100 4.6 7.9 1.0 CE1 C:PHE36 4.7 13.1 1.0 C C:LYS99 4.8 8.4 1.0 NE2 C:HIS103 4.8 9.5 1.0 CE2 C:PHE36 4.8 11.2 1.0 N C:LEU100 4.9 7.9 1.0 O D:HOH2174 5.0 22.6 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