Atomistry » Iron » PDB 4tof-4ud2 » 4u9g
Atomistry »
  Iron »
    PDB 4tof-4ud2 »
      4u9g »

Iron in PDB 4u9g: Crystal Structure of An H-Nox Protein From S. Oneidensis in the Fe(II)Co Ligation State, Q154A/Q155A/K156A Mutant

Protein crystallography data

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

Other elements in 4u9g:

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:

Zinc (Zn) 2 atoms
Sodium (Na) 1 atom

Iron Binding Sites:

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

Iron binding site 1 out of 2 in 4u9g

Go back to Iron Binding Sites List in 4u9g
Iron 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 Iron with other atoms in the Fe 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:Fe201

b:39.7
occ:1.00
FE A:HEM201 0.0 39.7 1.0
C A:CMO203 1.9 58.7 1.0
NB A:HEM201 2.0 40.0 1.0
NC A:HEM201 2.1 42.0 1.0
NA A:HEM201 2.1 38.8 1.0
ND A:HEM201 2.2 39.4 1.0
NE2 A:HIS103 2.2 36.2 1.0
C1B A:HEM201 3.0 37.9 1.0
C4A A:HEM201 3.0 38.2 1.0
CE1 A:HIS103 3.1 41.7 1.0
C4C A:HEM201 3.1 41.2 1.0
C4B A:HEM201 3.1 39.7 1.0
O A:CMO203 3.1 67.3 1.0
C1D A:HEM201 3.1 42.4 1.0
C1C A:HEM201 3.1 41.5 1.0
C1A A:HEM201 3.2 39.0 1.0
HE1 A:HIS103 3.2 50.0 1.0
C4D A:HEM201 3.2 41.8 1.0
CD2 A:HIS103 3.3 42.0 1.0
CHB A:HEM201 3.4 37.6 1.0
CHD A:HEM201 3.4 41.3 1.0
HD2 A:HIS103 3.5 50.4 1.0
CHC A:HEM201 3.5 40.4 1.0
CHA A:HEM201 3.6 38.8 1.0
C3A A:HEM201 4.2 39.8 1.0
ND1 A:HIS103 4.3 39.3 1.0
C2B A:HEM201 4.3 38.4 1.0
C2A A:HEM201 4.3 39.4 1.0
C3B A:HEM201 4.3 40.4 1.0
HHB A:HEM201 4.3 45.2 1.0
C3C A:HEM201 4.3 44.6 1.0
C2C A:HEM201 4.3 42.6 1.0
C2D A:HEM201 4.4 42.3 1.0
CG A:HIS103 4.4 43.0 1.0
C3D A:HEM201 4.4 40.9 1.0
HD13 A:LEU145 4.4 46.9 1.0
HHD A:HEM201 4.4 49.6 1.0
HD22 A:LEU115 4.4 53.0 1.0
HHC A:HEM201 4.5 48.5 1.0
HHA A:HEM201 4.5 46.6 1.0
HD13 A:LEU77 4.6 48.7 1.0
HD23 A:LEU115 4.7 53.0 1.0
HD22 A:LEU145 4.8 46.9 1.0
HD21 A:LEU115 4.9 53.0 1.0
CD2 A:LEU115 4.9 44.1 1.0
HG23 A:ILE98 4.9 49.4 1.0
HG22 A:ILE102 5.0 47.6 1.0

Iron binding site 2 out of 2 in 4u9g

Go back to Iron Binding Sites List in 4u9g
Iron 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 Iron with other atoms in the Fe 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:Fe201

b:53.8
occ:1.00
FE B:HEM201 0.0 53.8 1.0
NB B:HEM201 2.0 52.7 1.0
NA B:HEM201 2.1 47.8 1.0
NC B:HEM201 2.1 57.4 1.0
ND B:HEM201 2.1 51.5 1.0
NE2 B:HIS103 2.4 63.0 1.0
C1B B:HEM201 3.0 51.3 1.0
C4A B:HEM201 3.0 47.9 1.0
C4B B:HEM201 3.1 55.5 1.0
C1D B:HEM201 3.1 57.3 1.0
C1C B:HEM201 3.1 56.8 1.0
C1A B:HEM201 3.1 46.0 1.0
C4D B:HEM201 3.1 51.7 1.0
C4C B:HEM201 3.1 56.7 1.0
CE1 B:HIS103 3.2 59.6 1.0
HE1 B:HIS103 3.3 71.6 1.0
CHB B:HEM201 3.4 46.9 1.0
CHD B:HEM201 3.4 58.9 1.0
CD2 B:HIS103 3.4 67.4 1.0
CHC B:HEM201 3.5 55.4 1.0
CHA B:HEM201 3.5 46.5 1.0
HD2 B:HIS103 3.6 80.9 1.0
HD13 B:LEU145 3.8 68.3 1.0
HD13 B:LEU77 4.0 74.8 1.0
HHB B:HEM201 4.2 56.3 1.0
C3A B:HEM201 4.3 48.2 1.0
HD11 B:LEU77 4.3 74.8 1.0
C2B B:HEM201 4.3 50.1 1.0
C3B B:HEM201 4.3 56.0 1.0
C2A B:HEM201 4.3 42.1 1.0
C2C B:HEM201 4.3 59.4 1.0
C2D B:HEM201 4.3 53.5 1.0
C3C B:HEM201 4.3 58.4 1.0
C3D B:HEM201 4.3 49.0 1.0
HHD B:HEM201 4.4 70.7 1.0
ND1 B:HIS103 4.4 62.5 1.0
HHC B:HEM201 4.4 66.5 1.0
HHA B:HEM201 4.4 55.8 1.0
CD1 B:LEU77 4.5 62.4 1.0
HD22 B:LEU115 4.5 71.9 1.0
HD11 B:LEU145 4.5 68.3 1.0
CG B:HIS103 4.5 64.0 1.0
CD1 B:LEU145 4.6 56.9 1.0
HD12 B:LEU77 4.7 74.8 1.0
HD23 B:LEU115 4.9 71.9 1.0
HD22 B:LEU145 4.9 67.9 1.0
HG23 B:ILE98 5.0 73.7 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: Mon Aug 5 11:57:08 2024

Last articles

Zn in 9JPJ
Zn in 9JP7
Zn in 9JPK
Zn in 9JPL
Zn in 9GN6
Zn in 9GN7
Zn in 9GKU
Zn in 9GKW
Zn in 9GKX
Zn in 9GL0
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy