Zinc 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:

Manganese	(Mn)	2 atoms
Sodium	(Na)	1 atom

The binding sites of Zinc 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 Zinc atom.
In total 2 binding sites of Zinc 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 Zinc binding site number: 1; 2;

Zinc 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 Zinc with other atoms in the Zn 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:Zn202 b:47.6 occ:1.00 NE2 A:HIS161 2.0 49.9 1.0 SG A:CYS172 2.3 48.9 1.0 SG A:CYS139 2.3 47.2 1.0 SG A:CYS164 2.3 54.7 1.0 HE1 A:HIS161 2.6 62.0 1.0 CE1 A:HIS161 2.6 51.6 1.0 HB2 A:CYS139 2.9 56.8 1.0 CB A:CYS139 3.0 47.4 1.0 HA A:CYS164 3.0 62.4 1.0 HB3 A:CYS139 3.0 56.8 1.0 HB3 A:CYS172 3.1 56.4 1.0 CD2 A:HIS161 3.2 51.3 1.0 CB A:CYS164 3.2 52.2 1.0 HB2 A:CYS164 3.2 62.6 1.0 H A:MET165 3.3 61.8 1.0 CB A:CYS172 3.3 47.0 1.0 HD2 A:HIS166 3.6 73.6 1.0 CA A:CYS164 3.6 52.0 1.0 HD2 A:HIS161 3.6 61.6 1.0 HB2 A:CYS172 3.8 56.4 1.0 ND1 A:HIS161 3.9 52.9 1.0 N A:MET165 3.9 51.5 1.0 H A:HIS166 4.1 67.6 1.0 HB3 A:CYS164 4.1 62.6 1.0 CG A:HIS161 4.2 50.7 1.0 C A:CYS164 4.3 51.8 1.0 HE2 A:PHE140 4.4 60.3 1.0 HD12 A:LEU174 4.4 58.3 1.0 CA A:CYS139 4.5 47.0 1.0 O A:THR163 4.5 48.1 1.0 CD2 A:HIS166 4.5 61.4 1.0 HA A:CYS172 4.5 56.1 1.0 CA A:CYS172 4.6 46.8 1.0 HD1 A:HIS161 4.6 63.4 1.0 H A:CYS139 4.7 57.5 1.0 CE2 A:PHE140 4.7 50.3 1.0 HG3 A:MET165 4.7 59.8 1.0 HB2 A:MET165 4.7 62.4 1.0 HB2 A:HIS166 4.8 75.6 1.0 N A:CYS164 4.8 49.9 1.0 N A:HIS166 4.9 56.3 1.0 C A:CYS139 5.0 46.9 1.0

Zinc 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 Zinc with other atoms in the Zn 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:Zn202 b:56.0 occ:1.00 NE2 B:HIS161 2.1 65.1 1.0 SG B:CYS164 2.2 62.3 1.0 SG B:CYS139 2.3 57.1 1.0 SG B:CYS172 2.3 61.4 1.0 CE1 B:HIS161 2.8 63.0 1.0 HE1 B:HIS161 2.8 75.5 1.0 HB2 B:CYS139 2.9 66.8 1.0 CB B:CYS139 3.0 55.7 1.0 HB3 B:CYS172 3.0 77.1 1.0 HB3 B:CYS139 3.1 66.8 1.0 HA B:CYS164 3.1 79.3 1.0 CB B:CYS164 3.2 66.3 1.0 HB2 B:CYS164 3.2 79.6 1.0 CD2 B:HIS161 3.3 67.3 1.0 CB B:CYS172 3.3 64.2 1.0 H B:MET165 3.4 76.1 1.0 HD2 B:HIS166 3.6 73.2 1.0 HD2 B:HIS161 3.6 80.8 1.0 CA B:CYS164 3.6 66.1 1.0 HB2 B:CYS172 3.9 77.1 1.0 H B:HIS166 4.0 72.8 1.0 ND1 B:HIS161 4.0 65.9 1.0 N B:MET165 4.0 63.4 1.0 HB3 B:CYS164 4.1 79.6 1.0 CD2 B:HIS166 4.2 61.0 1.0 HA B:CYS172 4.2 77.3 1.0 CG B:HIS161 4.2 66.6 1.0 HD11 B:LEU174 4.3 83.2 1.0 C B:CYS164 4.3 66.7 1.0 CA B:CYS172 4.4 64.5 1.0 CA B:CYS139 4.5 55.5 1.0 HB2 B:HIS166 4.6 75.1 1.0 O B:THR163 4.7 71.2 1.0 HB2 B:MET165 4.7 69.7 1.0 HD1 B:HIS161 4.7 79.0 1.0 HG3 B:MET165 4.8 71.5 1.0 H B:CYS139 4.8 64.3 1.0 N B:HIS166 4.8 60.7 1.0 N B:CYS164 4.9 73.8 1.0 CG B:HIS166 4.9 60.9 1.0 NE2 B:HIS166 4.9 59.4 1.0 HD12 B:LEU174 5.0 83.2 1.0 HE2 B:HIS166 5.0 71.3 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