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Iron in PDB 1zvi: Rat Neuronal Nitric Oxide Synthase Oxygenase Domain

Enzymatic activity of Rat Neuronal Nitric Oxide Synthase Oxygenase Domain

All present enzymatic activity of Rat Neuronal Nitric Oxide Synthase Oxygenase Domain:
1.14.13.39;

Protein crystallography data

The structure of Rat Neuronal Nitric Oxide Synthase Oxygenase Domain, PDB code: 1zvi was solved by H.Matter, H.S.Kumar, R.Fedorov, A.Frey, P.Kotsonis, E.Hartmann, L.G.Frohlich, A.Reif, W.Pfleiderer, P.Scheurer, D.K.Ghosh, I.Schlichting, H.H.Schmidt, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 8.00 / 2.00
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 43.183, 107.522, 163.027, 90.00, 90.00, 90.00
R / Rfree (%) 19.9 / 25.5

Other elements in 1zvi:

The structure of Rat Neuronal Nitric Oxide Synthase Oxygenase Domain also contains other interesting chemical elements:

Zinc (Zn) 1 atom

Iron Binding Sites:

The binding sites of Iron atom in the Rat Neuronal Nitric Oxide Synthase Oxygenase Domain (pdb code 1zvi). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total only one binding site of Iron was determined in the Rat Neuronal Nitric Oxide Synthase Oxygenase Domain, PDB code: 1zvi:

Iron binding site 1 out of 1 in 1zvi

Go back to Iron Binding Sites List in 1zvi
Iron binding site 1 out of 1 in the Rat Neuronal Nitric Oxide Synthase Oxygenase Domain


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Rat Neuronal Nitric Oxide Synthase Oxygenase Domain within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe900

b:25.7
occ:1.00
FE A:HEM900 0.0 25.7 1.0
ND A:HEM900 1.9 17.6 1.0
NA A:HEM900 2.1 21.8 1.0
NB A:HEM900 2.1 27.9 1.0
NC A:HEM900 2.2 25.2 1.0
SG A:CYS415 2.3 21.9 1.0
C1D A:HEM900 2.9 22.9 1.0
C4D A:HEM900 3.0 23.9 1.0
C4A A:HEM900 3.1 22.2 1.0
C1B A:HEM900 3.1 32.1 1.0
C1A A:HEM900 3.1 25.8 1.0
C4C A:HEM900 3.1 25.4 1.0
C4B A:HEM900 3.1 27.4 1.0
C1C A:HEM900 3.2 26.1 1.0
CB A:CYS415 3.2 24.5 1.0
CHD A:HEM900 3.4 21.2 1.0
CHB A:HEM900 3.4 28.2 1.0
CHA A:HEM900 3.4 21.1 1.0
CHC A:HEM900 3.5 29.2 1.0
CA A:CYS415 4.0 28.3 1.0
C2D A:HEM900 4.2 26.0 1.0
C3D A:HEM900 4.2 24.7 1.0
C3A A:HEM900 4.3 28.6 1.0
C2A A:HEM900 4.3 27.4 1.0
C2B A:HEM900 4.4 31.0 1.0
NE1 A:TRP409 4.4 19.6 1.0
C3B A:HEM900 4.4 28.8 1.0
C2C A:HEM900 4.4 22.7 1.0
C3C A:HEM900 4.5 21.2 1.0
O A:HOH1141 4.5 38.5 1.0
C A:CYS415 4.8 26.6 1.0
N A:GLY417 4.8 27.7 1.0
N A:VAL416 4.9 22.1 1.0

Reference:

H.Matter, H.S.Kumar, R.Fedorov, A.Frey, P.Kotsonis, E.Hartmann, L.G.Frohlich, A.Reif, W.Pfleiderer, P.Scheurer, D.K.Ghosh, I.Schlichting, H.H.Schmidt. Structural Analysis of Isoform-Specific Inhibitors Targeting the Tetrahydrobiopterin Binding Site of Human Nitric Oxide Synthases. J.Med.Chem. V. 48 4783 2005.
ISSN: ISSN 0022-2623
PubMed: 16033258
DOI: 10.1021/JM050007X
Page generated: Sun Dec 13 14:39:05 2020

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