Iron 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
Sodium	(Na)	1 atom

The binding sites of Iron 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 Iron atom.
In total 2 binding sites of Iron where 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:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 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 Iron with other atoms in the Fe 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:Fe201 b:39.7 occ:1.00 FE A:HEM201 0.0 39.7 1.0 C A:CMO203 1.9 58.7 1.0 NB A:HEM201 2.0 40.0 1.0 NC A:HEM201 2.1 42.0 1.0 NA A:HEM201 2.1 38.8 1.0 ND A:HEM201 2.2 39.4 1.0 NE2 A:HIS103 2.2 36.2 1.0 C1B A:HEM201 3.0 37.9 1.0 C4A A:HEM201 3.0 38.2 1.0 CE1 A:HIS103 3.1 41.7 1.0 C4C A:HEM201 3.1 41.2 1.0 C4B A:HEM201 3.1 39.7 1.0 O A:CMO203 3.1 67.3 1.0 C1D A:HEM201 3.1 42.4 1.0 C1C A:HEM201 3.1 41.5 1.0 C1A A:HEM201 3.2 39.0 1.0 HE1 A:HIS103 3.2 50.0 1.0 C4D A:HEM201 3.2 41.8 1.0 CD2 A:HIS103 3.3 42.0 1.0 CHB A:HEM201 3.4 37.6 1.0 CHD A:HEM201 3.4 41.3 1.0 HD2 A:HIS103 3.5 50.4 1.0 CHC A:HEM201 3.5 40.4 1.0 CHA A:HEM201 3.6 38.8 1.0 C3A A:HEM201 4.2 39.8 1.0 ND1 A:HIS103 4.3 39.3 1.0 C2B A:HEM201 4.3 38.4 1.0 C2A A:HEM201 4.3 39.4 1.0 C3B A:HEM201 4.3 40.4 1.0 HHB A:HEM201 4.3 45.2 1.0 C3C A:HEM201 4.3 44.6 1.0 C2C A:HEM201 4.3 42.6 1.0 C2D A:HEM201 4.4 42.3 1.0 CG A:HIS103 4.4 43.0 1.0 C3D A:HEM201 4.4 40.9 1.0 HD13 A:LEU145 4.4 46.9 1.0 HHD A:HEM201 4.4 49.6 1.0 HD22 A:LEU115 4.4 53.0 1.0 HHC A:HEM201 4.5 48.5 1.0 HHA A:HEM201 4.5 46.6 1.0 HD13 A:LEU77 4.6 48.7 1.0 HD23 A:LEU115 4.7 53.0 1.0 HD22 A:LEU145 4.8 46.9 1.0 HD21 A:LEU115 4.9 53.0 1.0 CD2 A:LEU115 4.9 44.1 1.0 HG23 A:ILE98 4.9 49.4 1.0 HG22 A:ILE102 5.0 47.6 1.0

Iron binding site 2 out of 2 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 Iron with other atoms in the Fe binding site number 2 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 B:Fe201 b:53.8 occ:1.00 FE B:HEM201 0.0 53.8 1.0 NB B:HEM201 2.0 52.7 1.0 NA B:HEM201 2.1 47.8 1.0 NC B:HEM201 2.1 57.4 1.0 ND B:HEM201 2.1 51.5 1.0 NE2 B:HIS103 2.4 63.0 1.0 C1B B:HEM201 3.0 51.3 1.0 C4A B:HEM201 3.0 47.9 1.0 C4B B:HEM201 3.1 55.5 1.0 C1D B:HEM201 3.1 57.3 1.0 C1C B:HEM201 3.1 56.8 1.0 C1A B:HEM201 3.1 46.0 1.0 C4D B:HEM201 3.1 51.7 1.0 C4C B:HEM201 3.1 56.7 1.0 CE1 B:HIS103 3.2 59.6 1.0 HE1 B:HIS103 3.3 71.6 1.0 CHB B:HEM201 3.4 46.9 1.0 CHD B:HEM201 3.4 58.9 1.0 CD2 B:HIS103 3.4 67.4 1.0 CHC B:HEM201 3.5 55.4 1.0 CHA B:HEM201 3.5 46.5 1.0 HD2 B:HIS103 3.6 80.9 1.0 HD13 B:LEU145 3.8 68.3 1.0 HD13 B:LEU77 4.0 74.8 1.0 HHB B:HEM201 4.2 56.3 1.0 C3A B:HEM201 4.3 48.2 1.0 HD11 B:LEU77 4.3 74.8 1.0 C2B B:HEM201 4.3 50.1 1.0 C3B B:HEM201 4.3 56.0 1.0 C2A B:HEM201 4.3 42.1 1.0 C2C B:HEM201 4.3 59.4 1.0 C2D B:HEM201 4.3 53.5 1.0 C3C B:HEM201 4.3 58.4 1.0 C3D B:HEM201 4.3 49.0 1.0 HHD B:HEM201 4.4 70.7 1.0 ND1 B:HIS103 4.4 62.5 1.0 HHC B:HEM201 4.4 66.5 1.0 HHA B:HEM201 4.4 55.8 1.0 CD1 B:LEU77 4.5 62.4 1.0 HD22 B:LEU115 4.5 71.9 1.0 HD11 B:LEU145 4.5 68.3 1.0 CG B:HIS103 4.5 64.0 1.0 CD1 B:LEU145 4.6 56.9 1.0 HD12 B:LEU77 4.7 74.8 1.0 HD23 B:LEU115 4.9 71.9 1.0 HD22 B:LEU145 4.9 67.9 1.0 HG23 B:ILE98 5.0 73.7 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