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Zinc in PDB 4u9b: Crystal Structure of An H-Nox Protein From S. Oneidensis in the Fe(II)No Ligation State

Protein crystallography data

The structure of Crystal Structure of An H-Nox Protein From S. Oneidensis in the Fe(II)No Ligation State, PDB code: 4u9b 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) 33.82 / 1.65
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 67.636, 86.716, 33.822, 90.00, 90.00, 90.00
R / Rfree (%) 16.8 / 20.3

Other elements in 4u9b:

The structure of Crystal Structure of An H-Nox Protein From S. Oneidensis in the Fe(II)No Ligation State also contains other interesting chemical elements:

Iron (Fe) 1 atom

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of An H-Nox Protein From S. Oneidensis in the Fe(II)No Ligation State (pdb code 4u9b). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Crystal Structure of An H-Nox Protein From S. Oneidensis in the Fe(II)No Ligation State, PDB code: 4u9b:

Zinc binding site 1 out of 1 in 4u9b

Go back to Zinc Binding Sites List in 4u9b
Zinc binding site 1 out of 1 in the Crystal Structure of An H-Nox Protein From S. Oneidensis in the Fe(II)No Ligation State


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)No Ligation State within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn203

b:20.5
occ:1.00
NE2 A:HIS161 2.1 23.3 1.0
SG A:CYS164 2.3 21.6 1.0
SG A:CYS172 2.3 19.0 1.0
SG A:CYS139 2.3 20.1 1.0
HE1 A:HIS161 2.6 26.1 1.0
CE1 A:HIS161 2.7 21.8 1.0
HA A:CYS164 2.9 29.8 1.0
HB2 A:CYS139 2.9 21.2 1.0
HB3 A:CYS172 3.0 23.2 1.0
CB A:CYS139 3.1 17.6 1.0
HB3 A:CYS139 3.2 21.2 1.0
CB A:CYS164 3.2 22.8 1.0
H A:MET165 3.2 30.2 1.0
HB2 A:CYS164 3.3 27.3 1.0
CB A:CYS172 3.3 19.3 1.0
CD2 A:HIS161 3.4 24.1 1.0
HD2 A:HIS166 3.5 43.2 1.0
CA A:CYS164 3.5 24.8 1.0
HD2 A:HIS161 3.8 28.9 1.0
HB2 A:CYS172 3.9 23.2 1.0
N A:MET165 3.9 25.1 1.0
ND1 A:HIS161 3.9 21.7 1.0
H A:HIS166 4.0 33.3 1.0
HB3 A:CYS164 4.1 27.3 1.0
O A:HOH400 4.1 24.4 1.0
C A:CYS164 4.2 26.7 1.0
CD2 A:HIS166 4.2 36.0 1.0
CG A:HIS161 4.3 23.1 1.0
HE1 A:PHE140 4.3 33.0 1.0
O A:THR163 4.4 24.7 1.0
HD11 A:LEU174 4.4 28.5 1.0
HA A:CYS172 4.4 22.0 1.0
CA A:CYS172 4.5 18.3 1.0
HB2 A:MET165 4.5 28.1 1.0
HD1 A:PHE140 4.5 32.5 1.0
CA A:CYS139 4.5 15.5 1.0
HD1 A:HIS161 4.6 26.1 1.0
HG3 A:MET165 4.6 27.5 1.0
N A:CYS164 4.8 23.9 1.0
H A:CYS139 4.8 20.6 1.0
N A:HIS166 4.9 27.8 1.0
CE1 A:PHE140 4.9 27.5 1.0
HB2 A:HIS166 4.9 37.8 1.0
NE2 A:HIS166 4.9 35.6 1.0
CD1 A:PHE140 5.0 27.1 1.0
CA A:MET165 5.0 25.8 1.0
C A:THR163 5.0 25.9 1.0

Reference:

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
Page generated: Sun Oct 27 08:53:00 2024

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