Sodium in PDB 4u9g: Crystal Structure of An H-Nox Protein From S. Oneidensis in the Fe(II)Co Ligation State, Q154A/Q155A/K156A Mutant

The structure of Crystal Structure of An H-Nox Protein From S. Oneidensis in the Fe(II)Co Ligation State, Q154A/Q155A/K156A Mutant, PDB code: 4u9g was solved by M.A.Herzik Jr., R.Jonnalagadda, J.Kuriyan, M.A.Marletta, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	43.01 / 2.25
Space group	P 63 2 2
Cell size a, b, c (Å), α, β, γ (°)	164.173, 164.173, 102.366, 90.00, 90.00, 120.00
R / Rfree (%)	18.2 / 19.3

The structure of Crystal Structure of An H-Nox Protein From S. Oneidensis in the Fe(II)Co Ligation State, Q154A/Q155A/K156A Mutant also contains other interesting chemical elements:

Zinc	(Zn)	2 atoms
Iron	(Fe)	2 atoms

The binding sites of Sodium atom in the Crystal Structure of An H-Nox Protein From S. Oneidensis in the Fe(II)Co Ligation State, Q154A/Q155A/K156A Mutant (pdb code 4u9g). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total only one binding site of Sodium was determined in the Crystal Structure of An H-Nox Protein From S. Oneidensis in the Fe(II)Co Ligation State, Q154A/Q155A/K156A Mutant, PDB code: 4u9g:

Sodium binding site 1 out of 1 in the Crystal Structure of An H-Nox Protein From S. Oneidensis in the Fe(II)Co Ligation State, Q154A/Q155A/K156A Mutant


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Crystal Structure of An H-Nox Protein From S. Oneidensis in the Fe(II)Co Ligation State, Q154A/Q155A/K156A Mutant within 5.0Å range: probe atom residue distance (Å) B Occ A:Na204 b:50.2 occ:1.00 O A:HOH343 2.2 50.6 1.0 O A:LEU184 2.2 46.7 1.0 O A:HOH320 2.4 45.6 1.0 OD1 A:ASN180 2.4 63.9 1.0 O A:ASP181 2.5 50.7 1.0 O A:HOH327 2.6 41.5 1.0 HD22 A:ASN180 3.0 62.9 1.0 CG A:ASN180 3.3 56.0 1.0 C A:LEU184 3.4 45.3 1.0 H A:LEU184 3.4 59.1 1.0 ND2 A:ASN180 3.4 52.4 1.0 C A:ASP181 3.5 56.0 1.0 HA A:GLU182 3.6 74.5 1.0 H A:ASP181 3.7 58.2 1.0 HB3 A:LEU184 3.8 64.2 1.0 HA A:TYR185 3.9 58.9 1.0 N A:LEU184 4.0 49.3 1.0 N A:ASP181 4.1 48.5 1.0 CA A:LEU184 4.1 49.5 1.0 CA A:GLU182 4.2 62.0 1.0 C A:GLU182 4.3 56.9 1.0 N A:GLU182 4.3 53.4 1.0 HD21 A:ASN180 4.3 62.9 1.0 CB A:LEU184 4.4 53.5 1.0 CA A:ASP181 4.4 55.8 1.0 O A:HOH313 4.4 53.3 1.0 N A:TYR185 4.4 46.9 1.0 O A:GLU182 4.5 56.5 1.0 HB2 A:LEU184 4.6 64.2 1.0 HA A:ASP181 4.6 67.0 1.0 HA A:ASN180 4.6 61.9 1.0 CB A:ASN180 4.7 51.1 1.0 CA A:TYR185 4.7 49.1 1.0 N A:ASN183 4.7 51.6 1.0 H A:ASN183 4.9 62.0 1.0 C A:ASN180 4.9 52.3 1.0 CA A:ASN180 5.0 51.6 1.0

M.A.Herzik, R.Jonnalagadda, J.Kuriyan, M.A.Marletta. Structural Insights Into the Role of Iron-Histidine Bond Cleavage in Nitric Oxide-Induced Activation of H-Nox Gas Sensor Proteins. Proc.Natl.Acad.Sci.Usa V. 111 E4156 2014.
ISSN: ESSN 1091-6490
PubMed: 25253889
DOI: 10.1073/PNAS.1416936111