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Iron in PDB 1p6n: Bovine Endothelial Nos Heme Domain with L-N(Omega)-Nitroarginine-(4R)- Amino-L-Proline Amide Bound

Enzymatic activity of Bovine Endothelial Nos Heme Domain with L-N(Omega)-Nitroarginine-(4R)- Amino-L-Proline Amide Bound

All present enzymatic activity of Bovine Endothelial Nos Heme Domain with L-N(Omega)-Nitroarginine-(4R)- Amino-L-Proline Amide Bound:
1.14.13.39;

Protein crystallography data

The structure of Bovine Endothelial Nos Heme Domain with L-N(Omega)-Nitroarginine-(4R)- Amino-L-Proline Amide Bound, PDB code: 1p6n was solved by M.L.Flinspach, H.Li, J.Jamal, W.Yang, H.Huang, J.-M.Hah, J.A.Gomez-Vidal, E.A.Litzinger, R.B.Silverman, T.L.Poulos, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 42.55 / 2.50
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 57.669, 106.292, 156.524, 90.00, 90.00, 90.00
R / Rfree (%) 21.8 / 27.8

Other elements in 1p6n:

The structure of Bovine Endothelial Nos Heme Domain with L-N(Omega)-Nitroarginine-(4R)- Amino-L-Proline Amide Bound 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 Bovine Endothelial Nos Heme Domain with L-N(Omega)-Nitroarginine-(4R)- Amino-L-Proline Amide Bound (pdb code 1p6n). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Bovine Endothelial Nos Heme Domain with L-N(Omega)-Nitroarginine-(4R)- Amino-L-Proline Amide Bound, PDB code: 1p6n:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in 1p6n

Go back to Iron Binding Sites List in 1p6n
Iron binding site 1 out of 2 in the Bovine Endothelial Nos Heme Domain with L-N(Omega)-Nitroarginine-(4R)- Amino-L-Proline Amide Bound


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Bovine Endothelial Nos Heme Domain with L-N(Omega)-Nitroarginine-(4R)- Amino-L-Proline Amide Bound within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe500

b:33.5
occ:1.00
FE A:HEM500 0.0 33.5 1.0
NA A:HEM500 1.9 33.6 1.0
NB A:HEM500 2.0 30.7 1.0
NC A:HEM500 2.0 31.4 1.0
ND A:HEM500 2.0 31.9 1.0
SG A:CYS186 2.2 39.7 1.0
C1B A:HEM500 3.0 28.1 1.0
C1A A:HEM500 3.0 38.1 1.0
C4A A:HEM500 3.0 34.4 1.0
C4B A:HEM500 3.0 34.3 1.0
C1C A:HEM500 3.0 34.4 1.0
C4D A:HEM500 3.0 35.9 1.0
C4C A:HEM500 3.1 34.7 1.0
C1D A:HEM500 3.1 24.9 1.0
CB A:CYS186 3.3 42.9 1.0
CHB A:HEM500 3.4 32.5 1.0
CHC A:HEM500 3.4 34.8 1.0
CHA A:HEM500 3.4 34.0 1.0
CHD A:HEM500 3.4 30.4 1.0
NH1 A:DP9799 4.1 53.1 1.0
CA A:CYS186 4.1 39.6 1.0
C2A A:HEM500 4.2 37.2 1.0
C2B A:HEM500 4.2 33.7 1.0
C3A A:HEM500 4.3 34.6 1.0
C3D A:HEM500 4.3 36.3 1.0
C2C A:HEM500 4.3 30.1 1.0
C3B A:HEM500 4.3 33.3 1.0
C3C A:HEM500 4.3 35.6 1.0
C2D A:HEM500 4.3 35.1 1.0
NO A:DP9799 4.4 55.6 1.0
CZ A:DP9799 4.4 54.5 1.0
NE1 A:TRP180 4.5 34.2 1.0
O2 A:DP9799 4.6 55.5 1.0
NH2 A:DP9799 4.8 52.0 1.0
C A:CYS186 4.8 39.9 1.0
N A:GLY188 4.9 34.8 1.0
O3 A:DP9799 4.9 55.0 1.0

Iron binding site 2 out of 2 in 1p6n

Go back to Iron Binding Sites List in 1p6n
Iron binding site 2 out of 2 in the Bovine Endothelial Nos Heme Domain with L-N(Omega)-Nitroarginine-(4R)- Amino-L-Proline Amide Bound


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Bovine Endothelial Nos Heme Domain with L-N(Omega)-Nitroarginine-(4R)- Amino-L-Proline Amide Bound within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe500

b:37.1
occ:1.00
FE B:HEM500 0.0 37.1 1.0
NA B:HEM500 2.0 33.8 1.0
ND B:HEM500 2.0 31.9 1.0
NB B:HEM500 2.0 28.7 1.0
NC B:HEM500 2.0 27.1 1.0
SG B:CYS186 2.2 37.9 1.0
C1A B:HEM500 3.0 38.7 1.0
C4C B:HEM500 3.0 28.0 1.0
C1D B:HEM500 3.0 32.8 1.0
C1B B:HEM500 3.0 30.8 1.0
C1C B:HEM500 3.0 28.1 1.0
C4D B:HEM500 3.0 36.9 1.0
C4A B:HEM500 3.0 37.7 1.0
C4B B:HEM500 3.0 33.0 1.0
CHD B:HEM500 3.4 29.8 1.0
CHC B:HEM500 3.4 30.6 1.0
CHB B:HEM500 3.4 34.6 1.0
CHA B:HEM500 3.4 38.0 1.0
CB B:CYS186 3.5 40.3 1.0
NH1 B:DP9800 3.7 52.3 1.0
CZ B:DP9800 4.1 54.9 1.0
NO B:DP9800 4.2 48.8 1.0
CA B:CYS186 4.2 40.5 1.0
C2A B:HEM500 4.2 42.1 1.0
C2B B:HEM500 4.3 28.8 1.0
C2D B:HEM500 4.3 33.8 1.0
C3C B:HEM500 4.3 29.9 1.0
C3D B:HEM500 4.3 34.1 1.0
C2C B:HEM500 4.3 28.4 1.0
C3A B:HEM500 4.3 40.0 1.0
C3B B:HEM500 4.3 30.4 1.0
NH2 B:DP9800 4.4 58.1 1.0
NE1 B:TRP180 4.4 42.3 1.0
O2 B:DP9800 4.6 53.0 1.0
O3 B:DP9800 4.6 50.8 1.0
NE B:DP9800 4.8 54.3 1.0
N B:GLY188 4.8 40.4 1.0
N B:VAL187 4.9 41.8 1.0
C B:CYS186 4.9 43.2 1.0

Reference:

M.L.Flinspach, H.Li, J.Jamal, W.Yang, H.Huang, J.M.Hah, J.A.Gomez-Vidal, E.A.Litzinger, R.B.Silverman, T.L.Poulos. Structural Basis For Dipeptide Amide Isoform-Selective Inhibition of Neuronal Nitric Oxide Synthase. Nat.Struct.Mol.Biol. V. 11 54 2004.
ISSN: ISSN 1545-9993
PubMed: 14718923
DOI: 10.1038/NSMB704
Page generated: Sun Dec 13 14:27:49 2020

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