Atomistry » Arsenic » PDB 4cx1-4j8m » 4cx1
Atomistry »
  Arsenic »
    PDB 4cx1-4j8m »
      4cx1 »

Arsenic in PDB 4cx1: Structure of Bovine Endothelial Nitric Oxide Synthase L111A Mutant Heme Domain in Complex with 4-Methyl-6-(((3R,4R)-4-( (5-(4-Methylpyridin-2-Yl)Pentyl)Oxy)Pyrrolidin-3-Yl)Methyl) Pyridin-2-Amine

Enzymatic activity of Structure of Bovine Endothelial Nitric Oxide Synthase L111A Mutant Heme Domain in Complex with 4-Methyl-6-(((3R,4R)-4-( (5-(4-Methylpyridin-2-Yl)Pentyl)Oxy)Pyrrolidin-3-Yl)Methyl) Pyridin-2-Amine

All present enzymatic activity of Structure of Bovine Endothelial Nitric Oxide Synthase L111A Mutant Heme Domain in Complex with 4-Methyl-6-(((3R,4R)-4-( (5-(4-Methylpyridin-2-Yl)Pentyl)Oxy)Pyrrolidin-3-Yl)Methyl) Pyridin-2-Amine:
1.14.13.39;

Protein crystallography data

The structure of Structure of Bovine Endothelial Nitric Oxide Synthase L111A Mutant Heme Domain in Complex with 4-Methyl-6-(((3R,4R)-4-( (5-(4-Methylpyridin-2-Yl)Pentyl)Oxy)Pyrrolidin-3-Yl)Methyl) Pyridin-2-Amine, PDB code: 4cx1 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) 92.19 / 2.13
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 57.725, 106.199, 156.052, 90.00, 90.00, 90.00
R / Rfree (%) 17.243 / 21.428

Other elements in 4cx1:

The structure of Structure of Bovine Endothelial Nitric Oxide Synthase L111A Mutant Heme Domain in Complex with 4-Methyl-6-(((3R,4R)-4-( (5-(4-Methylpyridin-2-Yl)Pentyl)Oxy)Pyrrolidin-3-Yl)Methyl) Pyridin-2-Amine also contains other interesting chemical elements:

Iron (Fe) 2 atoms
Zinc (Zn) 1 atom

Arsenic Binding Sites:

The binding sites of Arsenic atom in the Structure of Bovine Endothelial Nitric Oxide Synthase L111A Mutant Heme Domain in Complex with 4-Methyl-6-(((3R,4R)-4-( (5-(4-Methylpyridin-2-Yl)Pentyl)Oxy)Pyrrolidin-3-Yl)Methyl) Pyridin-2-Amine (pdb code 4cx1). This binding sites where shown within 5.0 Angstroms radius around Arsenic atom.
In total 2 binding sites of Arsenic where determined in the Structure of Bovine Endothelial Nitric Oxide Synthase L111A Mutant Heme Domain in Complex with 4-Methyl-6-(((3R,4R)-4-( (5-(4-Methylpyridin-2-Yl)Pentyl)Oxy)Pyrrolidin-3-Yl)Methyl) Pyridin-2-Amine, PDB code: 4cx1:
Jump to Arsenic binding site number: 1; 2;

Arsenic binding site 1 out of 2 in 4cx1

Go back to Arsenic Binding Sites List in 4cx1
Arsenic binding site 1 out of 2 in the Structure of Bovine Endothelial Nitric Oxide Synthase L111A Mutant Heme Domain in Complex with 4-Methyl-6-(((3R,4R)-4-( (5-(4-Methylpyridin-2-Yl)Pentyl)Oxy)Pyrrolidin-3-Yl)Methyl) Pyridin-2-Amine


Mono view


Stereo pair view

A full contact list of Arsenic with other atoms in the As binding site number 1 of Structure of Bovine Endothelial Nitric Oxide Synthase L111A Mutant Heme Domain in Complex with 4-Methyl-6-(((3R,4R)-4-( (5-(4-Methylpyridin-2-Yl)Pentyl)Oxy)Pyrrolidin-3-Yl)Methyl) Pyridin-2-Amine within 5.0Å range:
probe atom residue distance (Å) B Occ
A:As384

b:65.9
occ:1.00
 AS A:CAS384 0.0 65.9 1.0
CE1 A:CAS384 2.0 55.1 1.0
CE2 A:CAS384 2.0 56.2 1.0
SG A:CAS384 2.5 43.0 1.0
CB A:CAS384 3.0 40.6 1.0
CA A:CAS384 3.7 40.7 1.0
CE3 A:TRP324 4.2 34.2 1.0
CD2 A:TRP324 4.3 35.7 1.0
CG A:TRP324 4.5 36.0 1.0
CB A:TRP324 4.6 37.7 1.0
N A:CAS384 4.7 39.6 1.0
C A:CAS384 4.7 41.7 1.0
O A:CAS384 4.8 42.9 1.0
CZ3 A:TRP324 4.9 34.1 1.0
CD1 A:LEU328 4.9 38.1 1.0

Arsenic binding site 2 out of 2 in 4cx1

Go back to Arsenic Binding Sites List in 4cx1
Arsenic binding site 2 out of 2 in the Structure of Bovine Endothelial Nitric Oxide Synthase L111A Mutant Heme Domain in Complex with 4-Methyl-6-(((3R,4R)-4-( (5-(4-Methylpyridin-2-Yl)Pentyl)Oxy)Pyrrolidin-3-Yl)Methyl) Pyridin-2-Amine


Mono view


Stereo pair view

A full contact list of Arsenic with other atoms in the As binding site number 2 of Structure of Bovine Endothelial Nitric Oxide Synthase L111A Mutant Heme Domain in Complex with 4-Methyl-6-(((3R,4R)-4-( (5-(4-Methylpyridin-2-Yl)Pentyl)Oxy)Pyrrolidin-3-Yl)Methyl) Pyridin-2-Amine within 5.0Å range:
probe atom residue distance (Å) B Occ
B:As384

b:91.8
occ:1.00
 AS B:CAS384 0.0 91.8 1.0
CE1 B:CAS384 2.0 86.3 1.0
CE2 B:CAS384 2.0 79.9 1.0
SG B:CAS384 2.6 64.8 1.0
CB B:CAS384 3.3 57.4 1.0
CA B:CAS384 4.0 57.0 1.0
CB B:TRP324 4.1 58.9 1.0
CE3 B:TRP324 4.2 53.4 1.0
CG B:TRP324 4.3 56.9 1.0
CD2 B:TRP324 4.3 54.1 1.0
CD2 B:LEU328 4.6 52.7 1.0
N B:CAS384 5.0 55.8 1.0

Reference:

H.Li, J.Jamal, S.L.Delker, C.Plaza, H.Ji, Q.Jing, H.Huang, S.Kang, R.B.Silverman, T.L.Poulos. Mobility of A Conserved Tyrosine Residue Controls Isoform- Dependent Enzyme-Inhibitor Interactions in Nitric Oxide Synthases. Biochemistry V. 53 5272 2014.
ISSN: ISSN 0006-2960
PubMed: 25089924
DOI: 10.1021/BI500561H
Page generated: Wed Jul 10 12:05:37 2024

Last articles

Zn in 7WTZ
Zn in 7WTX
Zn in 7WTW
Zn in 7WT5
Zn in 7WTU
Zn in 7WTV
Zn in 7WTT
Zn in 7WT4
Zn in 7WT3
Zn in 7WSS
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy