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Iron in PDB 4fvw: Structure of Rat Nnos Heme Domain in Complex with N(Omega)-Methoxy-L- Arginine

Enzymatic activity of Structure of Rat Nnos Heme Domain in Complex with N(Omega)-Methoxy-L- Arginine

All present enzymatic activity of Structure of Rat Nnos Heme Domain in Complex with N(Omega)-Methoxy-L- Arginine:
1.14.13.39;

Protein crystallography data

The structure of Structure of Rat Nnos Heme Domain in Complex with N(Omega)-Methoxy-L- Arginine, PDB code: 4fvw was solved by H.Li, T.L.Poulos, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 50.00 / 1.81
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 52.149, 111.003, 165.309, 90.00, 90.00, 90.00
R / Rfree (%) 18.1 / 21.8

Other elements in 4fvw:

The structure of Structure of Rat Nnos Heme Domain in Complex with N(Omega)-Methoxy-L- Arginine also contains other interesting chemical elements:

Zinc (Zn) 1 atom

Iron Binding Sites:

The binding sites of Iron atom in the Structure of Rat Nnos Heme Domain in Complex with N(Omega)-Methoxy-L- Arginine (pdb code 4fvw). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Structure of Rat Nnos Heme Domain in Complex with N(Omega)-Methoxy-L- Arginine, PDB code: 4fvw:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in 4fvw

Go back to Iron Binding Sites List in 4fvw
Iron binding site 1 out of 2 in the Structure of Rat Nnos Heme Domain in Complex with N(Omega)-Methoxy-L- Arginine


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Structure of Rat Nnos Heme Domain in Complex with N(Omega)-Methoxy-L- Arginine within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe801

b:30.5
occ:1.00
FE A:HEM801 0.0 30.5 1.0
NA A:HEM801 2.0 33.0 1.0
NC A:HEM801 2.0 27.7 1.0
ND A:HEM801 2.1 33.0 1.0
NB A:HEM801 2.1 33.1 1.0
SG A:CYS415 2.4 30.0 1.0
C4C A:HEM801 3.0 28.3 1.0
C1D A:HEM801 3.1 29.9 1.0
C4A A:HEM801 3.1 32.8 1.0
C1A A:HEM801 3.1 30.9 1.0
C1C A:HEM801 3.1 29.7 1.0
C4B A:HEM801 3.1 31.0 1.0
C1B A:HEM801 3.1 32.2 1.0
C4D A:HEM801 3.2 32.5 1.0
CHD A:HEM801 3.4 30.2 1.0
CB A:CYS415 3.4 29.1 1.0
CHB A:HEM801 3.5 30.5 1.0
CHC A:HEM801 3.5 31.7 1.0
CHA A:HEM801 3.6 31.7 1.0
NH1 A:1KJ803 3.9 49.2 1.0
CA A:CYS415 4.2 26.8 1.0
C3C A:HEM801 4.4 29.1 1.0
NE1 A:TRP409 4.4 31.8 1.0
C3A A:HEM801 4.4 31.7 1.0
C2A A:HEM801 4.4 31.0 1.0
C2D A:HEM801 4.4 31.8 1.0
C2C A:HEM801 4.4 30.6 1.0
C3B A:HEM801 4.4 34.5 1.0
C3D A:HEM801 4.4 33.5 1.0
C2B A:HEM801 4.5 32.7 1.0
C1 A:1KJ803 4.6 47.7 0.3
OH A:1KJ803 4.7 49.8 1.0
CZ A:1KJ803 4.7 41.9 1.0
C1 A:1KJ803 4.8 50.8 0.7
N A:GLY417 4.8 31.3 1.0
C A:CYS415 4.9 30.7 1.0
CD1 A:TRP409 5.0 29.2 1.0

Iron binding site 2 out of 2 in 4fvw

Go back to Iron Binding Sites List in 4fvw
Iron binding site 2 out of 2 in the Structure of Rat Nnos Heme Domain in Complex with N(Omega)-Methoxy-L- Arginine


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Structure of Rat Nnos Heme Domain in Complex with N(Omega)-Methoxy-L- Arginine within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe801

b:29.9
occ:1.00
FE B:HEM801 0.0 29.9 1.0
NC B:HEM801 2.0 27.7 1.0
NA B:HEM801 2.0 33.0 1.0
NB B:HEM801 2.1 31.1 1.0
ND B:HEM801 2.1 30.4 1.0
SG B:CYS415 2.4 28.0 1.0
C4C B:HEM801 3.0 26.9 1.0
C1D B:HEM801 3.0 30.1 1.0
C4B B:HEM801 3.1 31.4 1.0
C1A B:HEM801 3.1 28.5 1.0
C4D B:HEM801 3.1 29.6 1.0
C1C B:HEM801 3.1 26.4 1.0
C1B B:HEM801 3.1 31.3 1.0
C4A B:HEM801 3.1 31.0 1.0
CHD B:HEM801 3.4 30.2 1.0
CB B:CYS415 3.4 25.1 1.0
CHC B:HEM801 3.5 28.5 1.0
CHA B:HEM801 3.5 28.4 1.0
CHB B:HEM801 3.5 30.5 1.0
NH1 B:1KJ803 3.9 44.0 1.0
CA B:CYS415 4.2 26.4 1.0
C3C B:HEM801 4.3 28.3 1.0
C2D B:HEM801 4.4 30.1 1.0
C3B B:HEM801 4.4 34.5 1.0
C2C B:HEM801 4.4 27.8 1.0
C2A B:HEM801 4.4 30.7 1.0
C3D B:HEM801 4.4 30.4 1.0
C3A B:HEM801 4.4 30.5 1.0
NE1 B:TRP409 4.4 28.4 1.0
C2B B:HEM801 4.4 33.8 1.0
C1 B:1KJ803 4.5 45.9 0.3
CZ B:1KJ803 4.6 38.5 1.0
OH B:1KJ803 4.8 49.7 1.0
N B:GLY417 4.8 28.4 1.0
C B:CYS415 4.9 28.1 1.0
N B:VAL416 5.0 26.9 1.0

Reference:

K.Jansen Labby, H.Li, L.J.Roman, P.Martasek, T.L.Poulos, R.B.Silverman. Methylated N(Omega)-Hydroxy-L-Arginine Analogues As Mechanistic Probes For the Second Step of the Nitric Oxide Synthase-Catalyzed Reaction Biochemistry V. 52 3062 2013.
ISSN: ISSN 0006-2960
PubMed: 23586781
DOI: 10.1021/BI301571V
Page generated: Sun Dec 13 15:34:34 2020

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