Iron in PDB 4u99: Crystal Structure of An H-Nox Protein From S. Oneidensis in the Fe(II) Ligation State, Q154A/Q155A/K156A Mutant

The structure of Crystal Structure of An H-Nox Protein From S. Oneidensis in the Fe(II) Ligation State, Q154A/Q155A/K156A Mutant, PDB code: 4u99 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)	47.88 / 2.00
Space group	P 63 2 2
Cell size a, b, c (Å), α, β, γ (°)	164.003, 164.003, 101.718, 90.00, 90.00, 120.00
R / Rfree (%)	17.2 / 19.1

The structure of Crystal Structure of An H-Nox Protein From S. Oneidensis in the Fe(II) 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) Ligation State, Q154A/Q155A/K156A Mutant (pdb code 4u99). 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) Ligation State, Q154A/Q155A/K156A Mutant, PDB code: 4u99:
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) 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) Ligation State, Q154A/Q155A/K156A Mutant within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe201 b:35.0 occ:1.00 FE A:HEM201 0.0 35.0 1.0 NA A:HEM201 2.1 34.6 1.0 NB A:HEM201 2.1 35.4 1.0 NC A:HEM201 2.1 36.5 1.0 ND A:HEM201 2.1 34.4 1.0 NE2 A:HIS103 2.2 32.9 1.0 C4A A:HEM201 3.0 34.3 1.0 C1B A:HEM201 3.0 33.7 1.0 C4C A:HEM201 3.1 35.5 1.0 C1D A:HEM201 3.1 37.0 1.0 C1A A:HEM201 3.1 34.7 1.0 CE1 A:HIS103 3.1 38.4 1.0 C1C A:HEM201 3.1 35.8 1.0 C4B A:HEM201 3.1 34.7 1.0 C4D A:HEM201 3.1 36.8 1.0 HE1 A:HIS103 3.2 46.0 1.0 CD2 A:HIS103 3.3 38.6 1.0 CHB A:HEM201 3.4 33.9 1.0 CHD A:HEM201 3.4 35.7 1.0 HD2 A:HIS103 3.5 46.4 1.0 CHA A:HEM201 3.5 34.3 1.0 CHC A:HEM201 3.5 34.9 1.0 HD13 A:LEU145 3.9 42.6 1.0 HD13 A:LEU77 4.0 43.6 1.0 HHB A:HEM201 4.2 40.7 1.0 HD22 A:LEU115 4.2 49.1 1.0 C3A A:HEM201 4.3 35.8 1.0 ND1 A:HIS103 4.3 36.0 1.0 C2A A:HEM201 4.3 35.2 1.0 C2B A:HEM201 4.3 34.2 1.0 C3C A:HEM201 4.3 38.4 1.0 C3B A:HEM201 4.3 35.6 1.0 C2C A:HEM201 4.3 36.4 1.0 C2D A:HEM201 4.3 36.6 1.0 HHD A:HEM201 4.4 42.9 1.0 CG A:HIS103 4.4 39.7 1.0 C3D A:HEM201 4.4 35.5 1.0 HHA A:HEM201 4.4 41.1 1.0 HD11 A:LEU77 4.5 43.6 1.0 HHC A:HEM201 4.5 41.9 1.0 HD11 A:LEU145 4.6 42.6 1.0 CD1 A:LEU77 4.6 36.3 1.0 HD23 A:LEU115 4.6 49.1 1.0 CD1 A:LEU145 4.7 35.5 1.0 CD2 A:LEU115 4.8 40.9 1.0 HD21 A:LEU115 4.8 49.1 1.0 HD12 A:LEU77 4.8 43.6 1.0 HG23 A:ILE98 4.8 45.4 1.0 HG22 A:ILE102 4.9 43.5 1.0 HG21 A:VAL106 4.9 45.1 1.0 HG21 A:ILE102 4.9 43.5 1.0 HD2 A:PRO116 5.0 43.2 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) 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) Ligation State, Q154A/Q155A/K156A Mutant within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe201 b:51.8 occ:1.00 FE B:HEM201 0.0 51.8 1.0 NC B:HEM201 2.1 54.6 1.0 NB B:HEM201 2.1 51.4 1.0 NA B:HEM201 2.1 46.3 1.0 ND B:HEM201 2.1 48.6 1.0 NE2 B:HIS103 2.2 58.5 1.0 C4A B:HEM201 3.1 47.1 1.0 C1D B:HEM201 3.1 53.6 1.0 C4C B:HEM201 3.1 53.1 1.0 C1B B:HEM201 3.1 50.5 1.0 C1C B:HEM201 3.1 54.2 1.0 CE1 B:HIS103 3.1 55.1 1.0 C1A B:HEM201 3.1 44.5 1.0 C4B B:HEM201 3.1 54.2 1.0 C4D B:HEM201 3.1 48.8 1.0 HE1 B:HIS103 3.2 66.1 1.0 CD2 B:HIS103 3.3 62.6 1.0 CHD B:HEM201 3.4 54.9 1.0 CHB B:HEM201 3.4 46.4 1.0 HD2 B:HIS103 3.5 75.1 1.0 CHA B:HEM201 3.5 44.3 1.0 CHC B:HEM201 3.5 53.6 1.0 HD13 B:LEU145 3.9 63.4 1.0 HD13 B:LEU77 4.0 71.0 1.0 HD22 B:LEU115 4.2 65.7 1.0 ND1 B:HIS103 4.3 57.6 1.0 HHB B:HEM201 4.3 55.7 1.0 C3A B:HEM201 4.3 47.8 1.0 C2A B:HEM201 4.3 41.2 1.0 C3C B:HEM201 4.3 54.4 1.0 C2C B:HEM201 4.3 56.1 1.0 C2D B:HEM201 4.3 49.3 1.0 C2B B:HEM201 4.3 49.6 1.0 HHD B:HEM201 4.3 65.9 1.0 HD11 B:LEU77 4.3 71.0 1.0 C3B B:HEM201 4.3 55.3 1.0 C3D B:HEM201 4.3 45.5 1.0 CG B:HIS103 4.4 59.0 1.0 HHC B:HEM201 4.5 64.3 1.0 HHA B:HEM201 4.5 53.2 1.0 CD1 B:LEU77 4.5 59.2 1.0 HD11 B:LEU145 4.6 63.4 1.0 CD1 B:LEU145 4.7 52.8 1.0 HD23 B:LEU115 4.8 65.7 1.0 HD12 B:LEU77 4.8 71.0 1.0 CD2 B:LEU115 4.8 54.8 1.0 HG23 B:ILE98 4.9 68.3 1.0 HD2 B:PRO116 4.9 60.2 1.0 HG21 B:VAL106 4.9 84.4 1.0 HD21 B:LEU115 4.9 65.7 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