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Iron in PDB 1zzt: Bovine Enos N368D/V106M Double Mutant with L-N(Omega)- Nitroarginine-(4R)-Amino-L-Proline Amide Bound

Enzymatic activity of Bovine Enos N368D/V106M Double Mutant with L-N(Omega)- Nitroarginine-(4R)-Amino-L-Proline Amide Bound

All present enzymatic activity of Bovine Enos N368D/V106M Double Mutant with L-N(Omega)- Nitroarginine-(4R)-Amino-L-Proline Amide Bound:
1.14.13.39;

Protein crystallography data

The structure of Bovine Enos N368D/V106M Double Mutant with L-N(Omega)- Nitroarginine-(4R)-Amino-L-Proline Amide Bound, PDB code: 1zzt was solved by H.Li, M.L.Flinspach, J.Igarashi, J.Jamal, W.Yang, 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) 47.43 / 2.14
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 56.450, 105.740, 155.600, 90.00, 90.00, 90.00
R / Rfree (%) 18.9 / 23.3

Other elements in 1zzt:

The structure of Bovine Enos N368D/V106M Double Mutant 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 Enos N368D/V106M Double Mutant with L-N(Omega)- Nitroarginine-(4R)-Amino-L-Proline Amide Bound (pdb code 1zzt). 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 Enos N368D/V106M Double Mutant with L-N(Omega)- Nitroarginine-(4R)-Amino-L-Proline Amide Bound, PDB code: 1zzt:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in 1zzt

Go back to Iron Binding Sites List in 1zzt
Iron binding site 1 out of 2 in the Bovine Enos N368D/V106M Double Mutant 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 Enos N368D/V106M Double Mutant with L-N(Omega)- Nitroarginine-(4R)-Amino-L-Proline Amide Bound within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe700

b:28.1
occ:1.00
FE A:HEM700 0.0 28.1 1.0
ND A:HEM700 2.0 26.8 1.0
NB A:HEM700 2.0 26.1 1.0
NA A:HEM700 2.0 29.2 1.0
NC A:HEM700 2.0 26.4 1.0
SG A:CYS186 2.3 28.7 1.0
C1D A:HEM700 3.0 26.3 1.0
C1B A:HEM700 3.0 26.8 1.0
C4D A:HEM700 3.0 26.1 1.0
C4B A:HEM700 3.0 28.2 1.0
C1A A:HEM700 3.0 27.2 1.0
C4A A:HEM700 3.1 28.4 1.0
C4C A:HEM700 3.1 27.2 1.0
C1C A:HEM700 3.1 24.6 1.0
CB A:CYS186 3.3 27.0 1.0
CHD A:HEM700 3.4 29.3 1.0
CHA A:HEM700 3.4 26.7 1.0
CHB A:HEM700 3.4 28.5 1.0
CHC A:HEM700 3.5 27.5 1.0
CA A:CYS186 4.0 28.1 1.0
C3D A:HEM700 4.2 28.2 1.0
NH1 A:DP9799 4.2 38.5 1.0
C2B A:HEM700 4.2 28.6 1.0
C2D A:HEM700 4.3 31.5 1.0
C2A A:HEM700 4.3 26.9 1.0
C3B A:HEM700 4.3 29.4 1.0
NE1 A:TRP180 4.3 25.7 1.0
C3C A:HEM700 4.3 27.1 1.0
C3A A:HEM700 4.3 27.4 1.0
NO A:DP9799 4.3 34.7 1.0
C2C A:HEM700 4.3 24.2 1.0
CZ A:DP9799 4.5 36.0 1.0
O2 A:DP9799 4.6 38.4 1.0
O3 A:DP9799 4.7 38.9 1.0
N A:GLY188 4.7 30.1 1.0
C A:CYS186 4.8 30.9 1.0
NH2 A:DP9799 4.8 35.0 1.0
N A:VAL187 4.9 27.5 1.0
CD1 A:TRP180 4.9 26.3 1.0

Iron binding site 2 out of 2 in 1zzt

Go back to Iron Binding Sites List in 1zzt
Iron binding site 2 out of 2 in the Bovine Enos N368D/V106M Double Mutant 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 Enos N368D/V106M Double Mutant with L-N(Omega)- Nitroarginine-(4R)-Amino-L-Proline Amide Bound within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe700

b:31.0
occ:1.00
FE B:HEM700 0.0 31.0 1.0
NB B:HEM700 2.0 27.3 1.0
ND B:HEM700 2.0 29.4 1.0
NA B:HEM700 2.0 30.3 1.0
NC B:HEM700 2.0 26.9 1.0
SG B:CYS186 2.3 30.7 1.0
C1B B:HEM700 3.0 26.1 1.0
C4B B:HEM700 3.0 29.9 1.0
C4A B:HEM700 3.0 28.4 1.0
C1C B:HEM700 3.0 27.4 1.0
C1A B:HEM700 3.0 31.5 1.0
C1D B:HEM700 3.1 29.4 1.0
C4D B:HEM700 3.1 31.1 1.0
C4C B:HEM700 3.1 25.5 1.0
CB B:CYS186 3.3 32.3 1.0
CHC B:HEM700 3.4 28.5 1.0
CHB B:HEM700 3.4 26.2 1.0
CHD B:HEM700 3.4 29.9 1.0
CHA B:HEM700 3.4 29.6 1.0
NH1 B:DP9800 4.0 37.2 1.0
CA B:CYS186 4.0 29.6 1.0
NE1 B:TRP180 4.2 31.0 1.0
C2B B:HEM700 4.2 27.1 1.0
NO B:DP9800 4.2 34.6 1.0
C3A B:HEM700 4.3 31.8 1.0
C3B B:HEM700 4.3 28.2 1.0
C2A B:HEM700 4.3 31.3 1.0
C2D B:HEM700 4.3 29.4 1.0
C2C B:HEM700 4.3 27.8 1.0
C3D B:HEM700 4.3 30.3 1.0
C3C B:HEM700 4.3 30.7 1.0
CZ B:DP9800 4.5 36.3 1.0
O2 B:DP9800 4.5 32.7 1.0
O3 B:DP9800 4.7 36.5 1.0
N B:GLY188 4.8 29.8 1.0
C B:CYS186 4.8 28.2 1.0
CD1 B:TRP180 4.8 29.0 1.0
N B:VAL187 4.9 30.1 1.0
NH2 B:DP9800 4.9 34.0 1.0

Reference:

H.Li, M.L.Flinspach, J.Igarashi, J.Jamal, W.Yang, E.A.Litzinger, H.Huang, E.P.Erdal, R.B.Silverman, T.L.Poulos. Exploring the Binding Conformations of Bulkier Dipeptide Amide Inhibitors in Constitutive Nitric Oxide Synthases. Biochemistry V. 44 15222 2005.
ISSN: ISSN 0006-2960
PubMed: 16285725
DOI: 10.1021/BI0513610
Page generated: Sun Dec 13 14:39:14 2020

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