Zinc 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:

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) Ligation State, Q154A/Q155A/K156A Mutant (pdb code 4u99). 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) Ligation State, Q154A/Q155A/K156A Mutant, PDB code: 4u99:
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) 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) Ligation State, Q154A/Q155A/K156A Mutant within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn202 b:35.6 occ:1.00 NE2 A:HIS161 2.1 35.5 1.0 SG A:CYS172 2.3 37.0 1.0 SG A:CYS139 2.3 36.9 1.0 SG A:CYS164 2.4 39.6 1.0 HE1 A:HIS161 2.7 45.0 1.0 CE1 A:HIS161 2.7 37.5 1.0 HB2 A:CYS139 2.9 44.7 1.0 HB3 A:CYS172 3.0 42.4 1.0 CB A:CYS139 3.0 37.3 1.0 HA A:CYS164 3.0 47.3 1.0 HB3 A:CYS139 3.1 44.7 1.0 HB2 A:CYS164 3.2 44.9 1.0 CB A:CYS164 3.2 37.5 1.0 CB A:CYS172 3.2 35.3 1.0 CD2 A:HIS161 3.3 38.5 1.0 H A:MET165 3.3 45.3 1.0 HD2 A:HIS166 3.6 55.7 1.0 CA A:CYS164 3.6 39.4 1.0 HD2 A:HIS161 3.7 46.1 1.0 HB2 A:CYS172 3.7 42.4 1.0 O A:HOH392 3.9 41.8 1.0 ND1 A:HIS161 3.9 39.1 1.0 N A:MET165 4.0 37.7 1.0 HB3 A:CYS164 4.1 44.9 1.0 H A:HIS166 4.1 48.3 1.0 CG A:HIS161 4.2 36.5 1.0 C A:CYS164 4.3 38.1 1.0 HD11 A:LEU174 4.3 47.5 1.0 O A:THR163 4.4 35.8 1.0 HA A:CYS172 4.4 42.4 1.0 CD2 A:HIS166 4.5 46.4 1.0 CA A:CYS172 4.5 35.3 1.0 CA A:CYS139 4.5 36.5 1.0 HE2 A:PHE140 4.5 50.0 1.0 HD1 A:HIS161 4.6 47.0 1.0 HB2 A:MET165 4.6 46.3 1.0 HG3 A:MET165 4.7 45.0 1.0 H A:CYS139 4.7 45.3 1.0 CE2 A:PHE140 4.7 41.7 1.0 N A:CYS164 4.8 37.1 1.0 HB2 A:HIS166 4.8 54.9 1.0 O B:HOH325 4.9 39.2 1.0 N A:HIS166 5.0 40.3 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) 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) Ligation State, Q154A/Q155A/K156A Mutant within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn202 b:44.8 occ:1.00 NE2 B:HIS161 2.1 55.0 1.0 SG B:CYS172 2.2 50.2 1.0 SG B:CYS164 2.3 49.7 1.0 SG B:CYS139 2.3 46.1 1.0 HE1 B:HIS161 2.6 62.8 1.0 CE1 B:HIS161 2.7 52.3 1.0 HB2 B:CYS139 3.0 52.8 1.0 HA B:CYS164 3.0 62.6 1.0 CB B:CYS139 3.1 44.0 1.0 HB3 B:CYS172 3.1 63.4 1.0 HB3 B:CYS139 3.2 52.8 1.0 CB B:CYS164 3.2 53.2 1.0 HB2 B:CYS164 3.2 63.9 1.0 CD2 B:HIS161 3.3 56.3 1.0 H B:MET165 3.3 61.0 1.0 CB B:CYS172 3.3 52.8 1.0 HD2 B:HIS166 3.4 61.5 1.0 CA B:CYS164 3.6 52.2 1.0 HD2 B:HIS161 3.7 67.6 1.0 O B:HOH354 3.8 42.0 1.0 HB2 B:CYS172 3.9 63.4 1.0 N B:MET165 3.9 50.8 1.0 ND1 B:HIS161 3.9 56.0 1.0 H B:HIS166 4.0 55.1 1.0 HB3 B:CYS164 4.1 63.9 1.0 CD2 B:HIS166 4.1 51.2 1.0 C B:CYS164 4.2 54.0 1.0 CG B:HIS161 4.2 54.9 1.0 HA B:CYS172 4.3 61.0 1.0 HD11 B:LEU174 4.3 72.3 1.0 CA B:CYS172 4.5 50.8 1.0 CA B:CYS139 4.5 45.1 1.0 HB2 B:MET165 4.5 53.1 1.0 HD1 B:HIS161 4.6 67.1 1.0 O B:THR163 4.6 58.2 1.0 HE2 B:HIS166 4.8 60.7 1.0 NE2 B:HIS166 4.8 50.6 1.0 H B:CYS139 4.8 51.6 1.0 HB2 B:HIS166 4.8 59.2 1.0 N B:HIS166 4.8 45.9 1.0 N B:CYS164 4.8 62.2 1.0 HG3 B:MET165 4.8 56.8 1.0 CG B:HIS166 4.9 49.2 1.0 HD1 B:TYR132 5.0 57.6 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