Manganese in PDB 4u9j: Crystal Structure of An H-Nox Protein From S. Oneidensis in the Mn(II) Ligation State, Q154A/Q155A/K156A Mutant

The structure of Crystal Structure of An H-Nox Protein From S. Oneidensis in the Mn(II) Ligation State, Q154A/Q155A/K156A Mutant, PDB code: 4u9j 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)	48.03 / 2.10
Space group	P 63 2 2
Cell size a, b, c (Å), α, β, γ (°)	163.801, 163.801, 102.082, 90.00, 90.00, 120.00
R / Rfree (%)	17.1 / 19.7

The structure of Crystal Structure of An H-Nox Protein From S. Oneidensis in the Mn(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 Manganese atom in the Crystal Structure of An H-Nox Protein From S. Oneidensis in the Mn(II) Ligation State, Q154A/Q155A/K156A Mutant (pdb code 4u9j). 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) Ligation State, Q154A/Q155A/K156A Mutant, PDB code: 4u9j:
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) 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) Ligation State, Q154A/Q155A/K156A Mutant within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn201 b:40.8 occ:1.00 MN A:MNH201 0.0 40.8 1.0 ND A:MNH201 2.1 41.1 1.0 NA A:MNH201 2.1 40.3 1.0 NB A:MNH201 2.2 40.1 1.0 NE2 A:HIS103 2.2 37.0 1.0 NC A:MNH201 2.2 40.4 1.0 C4D A:MNH201 3.1 41.8 1.0 CE1 A:HIS103 3.1 42.5 1.0 C4A A:MNH201 3.1 39.4 1.0 C1A A:MNH201 3.2 40.4 1.0 C4B A:MNH201 3.2 40.2 1.0 C1B A:MNH201 3.2 39.9 1.0 C1D A:MNH201 3.2 41.3 1.0 C4C A:MNH201 3.2 40.5 1.0 HE1 A:HIS103 3.2 51.0 1.0 CD2 A:HIS103 3.2 42.5 1.0 CHB A:MNH201 3.2 39.8 1.0 CHA A:MNH201 3.2 41.1 1.0 C1C A:MNH201 3.3 40.7 1.0 CHD A:MNH201 3.3 40.5 1.0 CHC A:MNH201 3.4 40.5 1.0 HD2 A:HIS103 3.4 51.0 1.0 HD11 A:LEU145 4.0 47.9 1.0 HD12 A:LEU77 4.1 48.4 1.0 HD23 A:LEU115 4.2 53.1 1.0 HHA A:MNH201 4.2 49.3 1.0 HHB A:MNH201 4.2 47.7 1.0 HHD A:MNH201 4.2 48.7 1.0 ND1 A:HIS103 4.3 39.9 1.0 HHC A:MNH201 4.3 48.6 1.0 C3B A:MNH201 4.4 40.6 1.0 CG A:HIS103 4.4 43.5 1.0 C3D A:MNH201 4.4 42.1 1.0 C2A A:MNH201 4.4 39.3 1.0 C3A A:MNH201 4.4 38.4 1.0 C3C A:MNH201 4.4 40.6 1.0 C2D A:MNH201 4.5 41.7 1.0 C2B A:MNH201 4.5 40.1 1.0 HD13 A:LEU77 4.5 48.4 1.0 C2C A:MNH201 4.6 41.1 1.0 HD22 A:LEU115 4.6 53.1 1.0 HD21 A:LEU115 4.6 53.1 1.0 HG23 A:ILE98 4.6 50.6 1.0 CD2 A:LEU115 4.7 44.2 1.0 CD1 A:LEU77 4.7 40.3 1.0 HG21 A:VAL106 4.8 49.1 1.0 HG22 A:ILE102 4.8 48.2 1.0 HD2 A:PRO116 4.8 47.6 1.0 HD12 A:LEU145 4.8 47.9 1.0 HG23 A:ILE102 4.8 48.2 1.0 CD1 A:LEU145 4.8 39.9 1.0 HD11 A:LEU77 4.9 48.4 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) 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) Ligation State, Q154A/Q155A/K156A Mutant within 5.0Å range: probe atom residue distance (Å) B Occ B:Mn201 b:53.7 occ:1.00 MN B:MNH201 0.0 53.7 1.0 ND B:MNH201 2.1 54.0 1.0 NA B:MNH201 2.1 50.9 1.0 NB B:MNH201 2.2 55.3 1.0 NC B:MNH201 2.2 57.6 1.0 NE2 B:HIS103 2.3 59.1 1.0 C4D B:MNH201 3.0 52.4 1.0 C1A B:MNH201 3.1 48.9 1.0 CHA B:MNH201 3.1 50.1 1.0 C1D B:MNH201 3.2 56.9 1.0 C4A B:MNH201 3.2 50.6 1.0 CHD B:MNH201 3.2 58.9 1.0 C1B B:MNH201 3.2 55.3 1.0 C4C B:MNH201 3.2 59.6 1.0 CE1 B:HIS103 3.2 55.8 1.0 C4B B:MNH201 3.3 57.2 1.0 CHB B:MNH201 3.3 53.0 1.0 C1C B:MNH201 3.3 59.1 1.0 HE1 B:HIS103 3.3 66.9 1.0 CD2 B:HIS103 3.4 63.0 1.0 CHC B:MNH201 3.5 58.3 1.0 HD2 B:HIS103 3.6 75.6 1.0 HHA B:MNH201 4.0 60.1 1.0 HD13 B:LEU77 4.0 71.6 1.0 HD13 B:LEU145 4.1 62.5 1.0 HHD B:MNH201 4.1 70.6 1.0 HD23 B:LEU115 4.2 67.2 1.0 HHB B:MNH201 4.2 63.6 1.0 C3D B:MNH201 4.3 53.3 1.0 C2A B:MNH201 4.3 47.3 1.0 C3B B:MNH201 4.4 58.5 1.0 C2D B:MNH201 4.4 57.2 1.0 C3A B:MNH201 4.4 49.0 1.0 HHC B:MNH201 4.4 70.0 1.0 ND1 B:HIS103 4.4 58.0 1.0 HD11 B:LEU77 4.4 71.6 1.0 C3C B:MNH201 4.5 63.0 1.0 CG B:HIS103 4.5 59.2 1.0 C2B B:MNH201 4.5 57.4 1.0 C2C B:MNH201 4.6 62.2 1.0 CD1 B:LEU77 4.7 59.6 1.0 HD2 B:PRO116 4.7 62.3 1.0 HD11 B:LEU145 4.7 62.5 1.0 HD21 B:LEU115 4.8 67.2 1.0 CD2 B:LEU115 4.8 56.0 1.0 HG23 B:ILE98 4.8 69.6 1.0 HD22 B:LEU115 4.9 67.2 1.0 CD1 B:LEU145 4.9 52.1 1.0 HD12 B:LEU77 5.0 71.6 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