Zinc 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:

Iron	(Fe)	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 Fe(II)Co Ligation State, Q154A/Q155A/K156A Mutant (pdb code 4u9g). 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 Fe(II)Co Ligation State, Q154A/Q155A/K156A Mutant, PDB code: 4u9g:
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 Fe(II)Co 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 Fe(II)Co Ligation State, Q154A/Q155A/K156A Mutant within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn202 b:39.4 occ:1.00 NE2 A:HIS161 2.0 39.9 1.0 SG A:CYS172 2.3 41.3 1.0 SG A:CYS139 2.3 41.0 1.0 SG A:CYS164 2.3 43.9 1.0 HE1 A:HIS161 2.7 50.2 1.0 CE1 A:HIS161 2.7 41.8 1.0 HB2 A:CYS139 2.9 49.5 1.0 HB3 A:CYS172 2.9 47.7 1.0 CB A:CYS139 3.0 41.2 1.0 HA A:CYS164 3.0 52.6 1.0 HB3 A:CYS139 3.1 49.5 1.0 HB2 A:CYS164 3.2 50.2 1.0 CB A:CYS164 3.2 41.8 1.0 CB A:CYS172 3.2 39.8 1.0 CD2 A:HIS161 3.3 42.9 1.0 H A:MET165 3.3 50.5 1.0 CA A:CYS164 3.6 43.9 1.0 HD2 A:HIS161 3.6 51.5 1.0 HD2 A:HIS166 3.6 60.6 1.0 HB2 A:CYS172 3.7 47.7 1.0 O A:HOH368 3.9 39.3 1.0 ND1 A:HIS161 3.9 43.4 1.0 N A:MET165 3.9 42.0 1.0 HB3 A:CYS164 4.1 50.2 1.0 H A:HIS166 4.1 53.4 1.0 CG A:HIS161 4.2 40.9 1.0 C A:CYS164 4.3 42.5 1.0 HD11 A:LEU174 4.3 52.9 1.0 O A:THR163 4.4 40.4 1.0 HA A:CYS172 4.4 47.8 1.0 CA A:CYS172 4.5 39.8 1.0 CA A:CYS139 4.5 40.3 1.0 CD2 A:HIS166 4.5 50.5 1.0 HB2 A:MET165 4.6 51.3 1.0 HD1 A:HIS161 4.6 52.1 1.0 HE2 A:PHE140 4.6 55.4 1.0 HG3 A:MET165 4.7 50.1 1.0 H A:CYS139 4.8 49.8 1.0 O B:HOH323 4.8 40.8 1.0 N A:CYS164 4.8 41.8 1.0 HB2 A:HIS166 4.8 59.7 1.0 CE2 A:PHE140 4.8 46.2 1.0 N A:HIS166 5.0 44.5 1.0

Zinc 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 Zinc with other atoms in the Zn 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:Zn202 b:48.1 occ:1.00 NE2 B:HIS161 2.1 58.2 1.0 SG B:CYS172 2.3 53.5 1.0 SG B:CYS164 2.3 53.6 1.0 SG B:CYS139 2.4 49.2 1.0 HE1 B:HIS161 2.7 66.5 1.0 CE1 B:HIS161 2.7 55.4 1.0 HB2 B:CYS139 3.0 56.3 1.0 HA B:CYS164 3.1 67.7 1.0 CB B:CYS139 3.1 46.9 1.0 HB3 B:CYS172 3.2 67.4 1.0 HB3 B:CYS139 3.2 56.3 1.0 HB2 B:CYS164 3.2 68.9 1.0 CB B:CYS164 3.2 57.4 1.0 H B:MET165 3.3 65.8 1.0 CD2 B:HIS161 3.3 59.7 1.0 CB B:CYS172 3.4 56.1 1.0 HD2 B:HIS166 3.4 65.7 1.0 CA B:CYS164 3.6 56.4 1.0 HD2 B:HIS161 3.7 71.6 1.0 N B:MET165 3.9 54.9 1.0 H B:HIS166 3.9 60.2 1.0 ND1 B:HIS161 3.9 59.0 1.0 HB2 B:CYS172 4.0 67.4 1.0 CD2 B:HIS166 4.1 54.7 1.0 HB3 B:CYS164 4.1 68.9 1.0 C B:CYS164 4.2 58.3 1.0 CG B:HIS161 4.2 58.1 1.0 HA B:CYS172 4.4 65.2 1.0 HD11 B:LEU174 4.5 75.8 1.0 HB2 B:MET165 4.5 57.7 1.0 CA B:CYS172 4.5 54.3 1.0 CA B:CYS139 4.6 48.0 1.0 HD1 B:HIS161 4.6 70.8 1.0 O B:THR163 4.6 62.2 1.0 N B:HIS166 4.7 50.2 1.0 HB2 B:HIS166 4.7 64.2 1.0 NE2 B:HIS166 4.7 53.9 1.0 HE2 B:HIS166 4.7 64.7 1.0 HG3 B:MET165 4.8 61.3 1.0 H B:CYS139 4.8 55.2 1.0 N B:CYS164 4.9 66.7 1.0 CG B:HIS166 4.9 53.0 1.0 CA B:MET165 5.0 53.4 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