Manganese in PDB 4u9k: Crystal Structure of An H-Nox Protein From S. Oneidensis in the Mn(II)No Ligation State, Q154A/Q155A/K156A Mutant

The structure of Crystal Structure of An H-Nox Protein From S. Oneidensis in the Mn(II)No Ligation State, Q154A/Q155A/K156A Mutant, PDB code: 4u9k 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 / 2.45
Space group	P 63 2 2
Cell size a, b, c (Å), α, β, γ (°)	164.303, 164.303, 101.679, 90.00, 90.00, 120.00
R / Rfree (%)	18.2 / 20.7

The structure of Crystal Structure of An H-Nox Protein From S. Oneidensis in the Mn(II)No Ligation State, Q154A/Q155A/K156A Mutant also contains other interesting chemical elements:

Zinc	(Zn)	2 atoms
Sodium	(Na)	1 atom

The binding sites of Manganese atom in the Crystal Structure of An H-Nox Protein From S. Oneidensis in the Mn(II)No Ligation State, Q154A/Q155A/K156A Mutant (pdb code 4u9k). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the Crystal Structure of An H-Nox Protein From S. Oneidensis in the Mn(II)No Ligation State, Q154A/Q155A/K156A Mutant, PDB code: 4u9k:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in the Crystal Structure of An H-Nox Protein From S. Oneidensis in the Mn(II)No Ligation State, Q154A/Q155A/K156A Mutant


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Crystal Structure of An H-Nox Protein From S. Oneidensis in the Mn(II)No Ligation State, Q154A/Q155A/K156A Mutant within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn201 b:47.4 occ:1.00 MN A:MNH201 0.0 47.4 1.0 N A:NO203 1.6 47.8 1.0 ND A:MNH201 2.1 47.5 1.0 NA A:MNH201 2.1 46.8 1.0 NC A:MNH201 2.2 47.3 1.0 NE2 A:HIS103 2.2 45.3 1.0 NB A:MNH201 2.2 47.1 1.0 O A:NO203 2.9 70.2 1.0 C4D A:MNH201 3.1 47.9 1.0 C1A A:MNH201 3.1 46.7 1.0 CE1 A:HIS103 3.1 48.5 1.0 C4A A:MNH201 3.1 46.2 1.0 CHA A:MNH201 3.1 47.3 1.0 C1D A:MNH201 3.2 47.6 1.0 C4C A:MNH201 3.2 47.4 1.0 C4B A:MNH201 3.2 47.6 1.0 CHD A:MNH201 3.2 47.2 1.0 HE1 A:HIS103 3.2 58.2 1.0 C1C A:MNH201 3.2 47.9 1.0 CD2 A:HIS103 3.2 48.9 1.0 C1B A:MNH201 3.2 47.1 1.0 CHB A:MNH201 3.3 46.8 1.0 CHC A:MNH201 3.4 48.0 1.0 HD2 A:HIS103 3.5 58.7 1.0 HD11 A:LEU145 3.9 55.8 1.0 HD12 A:LEU77 4.0 57.0 1.0 HHA A:MNH201 4.0 56.8 1.0 HHD A:MNH201 4.1 56.6 1.0 HHB A:MNH201 4.2 56.2 1.0 HD13 A:LEU77 4.2 57.0 1.0 ND1 A:HIS103 4.2 47.6 1.0 HHC A:MNH201 4.3 57.6 1.0 C3D A:MNH201 4.3 48.1 1.0 C2A A:MNH201 4.3 45.7 1.0 C3A A:MNH201 4.3 45.1 1.0 C3B A:MNH201 4.4 47.9 1.0 CG A:HIS103 4.4 49.9 1.0 C3C A:MNH201 4.4 48.0 1.0 C2D A:MNH201 4.4 47.9 1.0 HD23 A:LEU115 4.4 61.7 1.0 CD1 A:LEU77 4.5 47.5 1.0 C2C A:MNH201 4.5 48.6 1.0 C2B A:MNH201 4.5 47.4 1.0 HD11 A:LEU77 4.6 57.0 1.0 HD22 A:LEU145 4.6 56.2 1.0 HD12 A:LEU145 4.6 55.8 1.0 CD1 A:LEU145 4.7 46.5 1.0 HD21 A:LEU115 4.8 61.7 1.0 HD22 A:LEU115 4.9 61.7 1.0 HG23 A:ILE98 4.9 57.4 1.0 CD2 A:LEU115 4.9 51.4 1.0 HD1 A:HIS103 5.0 57.1 1.0

Manganese binding site 2 out of 2 in the Crystal Structure of An H-Nox Protein From S. Oneidensis in the Mn(II)No Ligation State, Q154A/Q155A/K156A Mutant


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Crystal Structure of An H-Nox Protein From S. Oneidensis in the Mn(II)No Ligation State, Q154A/Q155A/K156A Mutant within 5.0Å range: probe atom residue distance (Å) B Occ B:Mn201 b:62.4 occ:1.00 MN B:MNH201 0.0 62.4 1.0 ND B:MNH201 2.1 62.3 1.0 NA B:MNH201 2.1 59.6 1.0 NC B:MNH201 2.2 67.8 1.0 NB B:MNH201 2.2 64.8 1.0 NE2 B:HIS103 2.3 68.9 1.0 C1A B:MNH201 3.0 57.0 1.0 C4A B:MNH201 3.1 59.7 1.0 CE1 B:HIS103 3.1 66.1 1.0 C4D B:MNH201 3.1 60.2 1.0 C1D B:MNH201 3.1 65.7 1.0 CHD B:MNH201 3.1 68.4 1.0 HE1 B:HIS103 3.2 79.3 1.0 CHA B:MNH201 3.2 57.6 1.0 C4C B:MNH201 3.2 69.7 1.0 C4B B:MNH201 3.2 67.3 1.0 C1B B:MNH201 3.3 65.0 1.0 C1C B:MNH201 3.3 69.6 1.0 CHB B:MNH201 3.3 62.5 1.0 CD2 B:HIS103 3.4 71.7 1.0 CHC B:MNH201 3.4 68.8 1.0 HD2 B:HIS103 3.6 86.1 1.0 HD13 B:LEU145 3.8 75.3 1.0 HD13 B:LEU77 3.9 83.1 1.0 HHA B:MNH201 4.0 69.2 1.0 HHD B:MNH201 4.1 82.1 1.0 HD11 B:LEU77 4.1 83.1 1.0 HHB B:MNH201 4.2 75.0 1.0 C2A B:MNH201 4.2 55.2 1.0 ND1 B:HIS103 4.3 67.5 1.0 C3A B:MNH201 4.3 57.5 1.0 HD11 B:LEU145 4.3 75.3 1.0 C3D B:MNH201 4.3 61.4 1.0 HHC B:MNH201 4.3 82.6 1.0 C2D B:MNH201 4.4 65.6 1.0 C3C B:MNH201 4.4 73.2 1.0 CD1 B:LEU77 4.4 69.2 1.0 C3B B:MNH201 4.4 68.6 1.0 CG B:HIS103 4.4 69.1 1.0 C2C B:MNH201 4.5 72.7 1.0 CD1 B:LEU145 4.5 62.8 1.0 C2B B:MNH201 4.6 67.7 1.0 HD12 B:LEU77 4.7 83.1 1.0 HD23 B:LEU115 4.7 78.3 1.0 HD22 B:LEU145 4.8 76.5 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