Atomistry » Iron » PDB 4cuo-4d36 » 4cvg
Atomistry »
  Iron »
    PDB 4cuo-4d36 »
      4cvg »

Iron in PDB 4cvg: Structure of Bovine Endothelial Nitric Oxide Synthase Heme Domain (H4B-Free) Supplemented with 50UM Zn Acetate and with Poor Binding of 6-Acetyl-2-Amino-7,7-Dimethyl-7,8-Dihydropteridin-4(3H)-One.

Enzymatic activity of Structure of Bovine Endothelial Nitric Oxide Synthase Heme Domain (H4B-Free) Supplemented with 50UM Zn Acetate and with Poor Binding of 6-Acetyl-2-Amino-7,7-Dimethyl-7,8-Dihydropteridin-4(3H)-One.

All present enzymatic activity of Structure of Bovine Endothelial Nitric Oxide Synthase Heme Domain (H4B-Free) Supplemented with 50UM Zn Acetate and with Poor Binding of 6-Acetyl-2-Amino-7,7-Dimethyl-7,8-Dihydropteridin-4(3H)-One.:
1.14.13.39;

Protein crystallography data

The structure of Structure of Bovine Endothelial Nitric Oxide Synthase Heme Domain (H4B-Free) Supplemented with 50UM Zn Acetate and with Poor Binding of 6-Acetyl-2-Amino-7,7-Dimethyl-7,8-Dihydropteridin-4(3H)-One., PDB code: 4cvg was solved by G.Chreifi, 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 / 2.31
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 57.414, 105.957, 156.530, 90.00, 90.00, 90.00
R / Rfree (%) 15.479 / 21.358

Other elements in 4cvg:

The structure of Structure of Bovine Endothelial Nitric Oxide Synthase Heme Domain (H4B-Free) Supplemented with 50UM Zn Acetate and with Poor Binding of 6-Acetyl-2-Amino-7,7-Dimethyl-7,8-Dihydropteridin-4(3H)-One. also contains other interesting chemical elements:

Arsenic (As) 2 atoms
Zinc (Zn) 1 atom

Iron Binding Sites:

The binding sites of Iron atom in the Structure of Bovine Endothelial Nitric Oxide Synthase Heme Domain (H4B-Free) Supplemented with 50UM Zn Acetate and with Poor Binding of 6-Acetyl-2-Amino-7,7-Dimethyl-7,8-Dihydropteridin-4(3H)-One. (pdb code 4cvg). 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 Bovine Endothelial Nitric Oxide Synthase Heme Domain (H4B-Free) Supplemented with 50UM Zn Acetate and with Poor Binding of 6-Acetyl-2-Amino-7,7-Dimethyl-7,8-Dihydropteridin-4(3H)-One., PDB code: 4cvg:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in 4cvg

Go back to Iron Binding Sites List in 4cvg
Iron binding site 1 out of 2 in the Structure of Bovine Endothelial Nitric Oxide Synthase Heme Domain (H4B-Free) Supplemented with 50UM Zn Acetate and with Poor Binding of 6-Acetyl-2-Amino-7,7-Dimethyl-7,8-Dihydropteridin-4(3H)-One.


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Structure of Bovine Endothelial Nitric Oxide Synthase Heme Domain (H4B-Free) Supplemented with 50UM Zn Acetate and with Poor Binding of 6-Acetyl-2-Amino-7,7-Dimethyl-7,8-Dihydropteridin-4(3H)-One. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe500

b:33.7
occ:1.00
 FE A:HEM500 0.0 33.7 1.0
ND A:HEM500 1.9 28.8 1.0
NA A:HEM500 2.0 35.4 1.0
NB A:HEM500 2.0 26.2 1.0
NC A:HEM500 2.0 31.6 1.0
SG A:CYS186 2.3 38.6 1.0
C4D A:HEM500 2.9 29.9 1.0
C1D A:HEM500 2.9 31.3 1.0
C4B A:HEM500 2.9 33.2 1.0
C1B A:HEM500 3.0 32.5 1.0
C1A A:HEM500 3.0 32.7 1.0
C1C A:HEM500 3.0 31.3 1.0
C4C A:HEM500 3.1 34.0 1.0
C4A A:HEM500 3.1 33.8 1.0
CHA A:HEM500 3.4 30.9 1.0
CB A:CYS186 3.4 36.7 1.0
CHC A:HEM500 3.4 33.3 1.0
CHD A:HEM500 3.4 31.9 1.0
CHB A:HEM500 3.5 33.3 1.0
NH2 A:ARG700 4.1 59.1 1.0
CA A:CYS186 4.1 34.1 1.0
CZ A:ARG700 4.2 70.6 1.0
C3D A:HEM500 4.2 30.6 1.0
C2D A:HEM500 4.2 30.8 1.0
C2B A:HEM500 4.2 30.6 1.0
C3B A:HEM500 4.2 32.6 1.0
C2C A:HEM500 4.2 32.9 1.0
C2A A:HEM500 4.2 36.1 1.0
C3C A:HEM500 4.2 31.1 1.0
C3A A:HEM500 4.3 35.2 1.0
NE1 A:TRP180 4.4 32.5 1.0
NH1 A:ARG700 4.5 59.5 1.0
NE A:ARG700 4.5 69.2 1.0
N A:GLY188 4.8 32.4 1.0
C A:CYS186 4.9 34.0 1.0
N A:VAL187 4.9 33.2 1.0
CD A:ARG700 5.0 77.6 1.0

Iron binding site 2 out of 2 in 4cvg

Go back to Iron Binding Sites List in 4cvg
Iron binding site 2 out of 2 in the Structure of Bovine Endothelial Nitric Oxide Synthase Heme Domain (H4B-Free) Supplemented with 50UM Zn Acetate and with Poor Binding of 6-Acetyl-2-Amino-7,7-Dimethyl-7,8-Dihydropteridin-4(3H)-One.


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Structure of Bovine Endothelial Nitric Oxide Synthase Heme Domain (H4B-Free) Supplemented with 50UM Zn Acetate and with Poor Binding of 6-Acetyl-2-Amino-7,7-Dimethyl-7,8-Dihydropteridin-4(3H)-One. within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe500

b:37.7
occ:1.00
 FE B:HEM500 0.0 37.7 1.0
ND B:HEM500 1.9 42.5 1.0
NA B:HEM500 2.0 40.3 1.0
NB B:HEM500 2.1 37.4 1.0
NC B:HEM500 2.1 37.4 1.0
SG B:CYS186 2.3 35.8 1.0
C1D B:HEM500 3.0 43.5 1.0
C4D B:HEM500 3.0 41.8 1.0
C1A B:HEM500 3.0 41.1 1.0
C4A B:HEM500 3.0 37.4 1.0
C4B B:HEM500 3.0 40.7 1.0
C4C B:HEM500 3.1 35.4 1.0
C1B B:HEM500 3.1 38.3 1.0
C1C B:HEM500 3.1 38.7 1.0
CHB B:HEM500 3.4 35.0 1.0
CHC B:HEM500 3.4 40.2 1.0
CHD B:HEM500 3.4 36.1 1.0
CHA B:HEM500 3.4 35.1 1.0
CB B:CYS186 3.5 38.2 1.0
NH2 B:ARG700 3.7 69.3 1.0
CZ B:ARG700 4.0 77.5 1.0
CA B:CYS186 4.2 39.4 1.0
C2A B:HEM500 4.2 48.6 1.0
C3A B:HEM500 4.2 41.8 1.0
C3D B:HEM500 4.2 42.9 1.0
C2D B:HEM500 4.2 44.2 1.0
C3C B:HEM500 4.3 37.4 1.0
C2C B:HEM500 4.3 42.4 1.0
C2B B:HEM500 4.3 38.6 1.0
C3B B:HEM500 4.3 40.7 1.0
NE1 B:TRP180 4.4 36.8 1.0
NE B:ARG700 4.5 72.8 1.0
NH1 B:ARG700 4.5 64.0 1.0
CD B:ARG700 4.9 77.2 1.0
N B:GLY188 4.9 35.2 1.0
C B:CYS186 4.9 36.1 1.0
N B:VAL187 5.0 37.9 1.0

Reference:

G.Chreifi, H.Li, C.R.Mcinnes, C.L.Gibson, C.J.Suckling, T.L.Poulos. Communication Between the Zinc and Tetrahydrobiopterin Binding Sites in Nitric Oxide Synthase. Biochemistry V. 53 4216 2014.
ISSN: ISSN 0006-2960
PubMed: 24819538
DOI: 10.1021/BI5003986
Page generated: Sun Dec 13 15:30:43 2020

Last articles

Zn in 8WB0
Zn in 8WAX
Zn in 8WAU
Zn in 8WAZ
Zn in 8WAY
Zn in 8WAV
Zn in 8WAW
Zn in 8WAT
Zn in 8W7M
Zn in 8WD3
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy