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Iron in PDB 1q2o: Bovine Endothelial Nitric Oxide Synthase N368D Mutant Heme Domain Dimer with L-N(Omega)-Nitroarginine-2,4-L-Diaminobutyramide Bound

Enzymatic activity of Bovine Endothelial Nitric Oxide Synthase N368D Mutant Heme Domain Dimer with L-N(Omega)-Nitroarginine-2,4-L-Diaminobutyramide Bound

All present enzymatic activity of Bovine Endothelial Nitric Oxide Synthase N368D Mutant Heme Domain Dimer with L-N(Omega)-Nitroarginine-2,4-L-Diaminobutyramide Bound:
1.14.13.39;

Protein crystallography data

The structure of Bovine Endothelial Nitric Oxide Synthase N368D Mutant Heme Domain Dimer with L-N(Omega)-Nitroarginine-2,4-L-Diaminobutyramide Bound, PDB code: 1q2o 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) 48.44 / 1.74
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 57.908, 106.989, 156.989, 90.00, 90.00, 90.00
R / Rfree (%) 19.3 / 22

Other elements in 1q2o:

The structure of Bovine Endothelial Nitric Oxide Synthase N368D Mutant Heme Domain Dimer with L-N(Omega)-Nitroarginine-2,4-L-Diaminobutyramide 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 Nitric Oxide Synthase N368D Mutant Heme Domain Dimer with L-N(Omega)-Nitroarginine-2,4-L-Diaminobutyramide Bound (pdb code 1q2o). 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 Nitric Oxide Synthase N368D Mutant Heme Domain Dimer with L-N(Omega)-Nitroarginine-2,4-L-Diaminobutyramide Bound, PDB code: 1q2o:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in 1q2o

Go back to Iron Binding Sites List in 1q2o
Iron binding site 1 out of 2 in the Bovine Endothelial Nitric Oxide Synthase N368D Mutant Heme Domain Dimer with L-N(Omega)-Nitroarginine-2,4-L-Diaminobutyramide 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 Nitric Oxide Synthase N368D Mutant Heme Domain Dimer with L-N(Omega)-Nitroarginine-2,4-L-Diaminobutyramide Bound within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe700

b:15.8
occ:1.00
FE A:HEM700 0.0 15.8 1.0
NA A:HEM700 2.0 16.5 1.0
ND A:HEM700 2.0 15.3 1.0
NB A:HEM700 2.0 16.3 1.0
NC A:HEM700 2.0 15.3 1.0
SG A:CYS186 2.3 15.3 1.0
C1D A:HEM700 3.1 16.0 1.0
C1C A:HEM700 3.1 13.6 1.0
C1A A:HEM700 3.1 15.3 1.0
C1B A:HEM700 3.1 16.2 1.0
C4A A:HEM700 3.1 15.4 1.0
C4D A:HEM700 3.1 16.1 1.0
C4C A:HEM700 3.1 15.6 1.0
C4B A:HEM700 3.1 16.6 1.0
CB A:CYS186 3.4 15.0 1.0
CHB A:HEM700 3.5 16.0 1.0
CHC A:HEM700 3.5 15.2 1.0
CHD A:HEM700 3.5 14.3 1.0
CHA A:HEM700 3.5 15.8 1.0
NH1 A:DP1790 3.9 29.4 0.5
CA A:CYS186 4.1 15.5 1.0
C2D A:HEM700 4.3 16.5 1.0
C2A A:HEM700 4.3 16.1 1.0
C3D A:HEM700 4.3 17.8 1.0
C2B A:HEM700 4.3 15.5 1.0
C2C A:HEM700 4.3 15.2 1.0
C3A A:HEM700 4.3 14.9 1.0
C3C A:HEM700 4.3 15.4 1.0
NE1 A:TRP180 4.3 15.2 1.0
NO A:DP1790 4.3 29.6 0.5
C3B A:HEM700 4.3 16.3 1.0
NH1 A:DP1790 4.4 22.0 0.5
NO A:DP1790 4.5 22.8 0.5
CZ A:DP1790 4.5 29.0 0.5
CZ A:DP1790 4.6 22.5 0.5
O2 A:DP1790 4.7 29.8 0.5
O3 A:DP1790 4.8 28.5 0.5
O3 A:DP1790 4.8 20.9 0.5
NH2 A:DP1790 4.8 19.7 0.5
C A:CYS186 4.8 16.1 1.0
N A:GLY188 4.8 15.6 1.0
O2 A:DP1790 4.8 23.3 0.5
NH2 A:DP1790 4.9 26.9 0.5
CD1 A:TRP180 4.9 15.1 1.0
N A:VAL187 5.0 15.9 1.0

Iron binding site 2 out of 2 in 1q2o

Go back to Iron Binding Sites List in 1q2o
Iron binding site 2 out of 2 in the Bovine Endothelial Nitric Oxide Synthase N368D Mutant Heme Domain Dimer with L-N(Omega)-Nitroarginine-2,4-L-Diaminobutyramide 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 Nitric Oxide Synthase N368D Mutant Heme Domain Dimer with L-N(Omega)-Nitroarginine-2,4-L-Diaminobutyramide Bound within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe700

b:16.6
occ:1.00
FE B:HEM700 0.0 16.6 1.0
ND B:HEM700 2.0 16.6 1.0
NB B:HEM700 2.0 17.1 1.0
NA B:HEM700 2.0 15.2 1.0
NC B:HEM700 2.0 15.8 1.0
SG B:CYS186 2.3 15.5 1.0
C1B B:HEM700 3.1 15.4 1.0
C4D B:HEM700 3.1 16.6 1.0
C1A B:HEM700 3.1 15.5 1.0
C4A B:HEM700 3.1 15.4 1.0
C1D B:HEM700 3.1 14.1 1.0
C4C B:HEM700 3.1 14.2 1.0
C1C B:HEM700 3.1 15.3 1.0
C4B B:HEM700 3.1 16.2 1.0
CB B:CYS186 3.4 17.0 1.0
CHD B:HEM700 3.4 14.8 1.0
CHB B:HEM700 3.5 14.7 1.0
CHA B:HEM700 3.5 15.2 1.0
CHC B:HEM700 3.5 15.9 1.0
CA B:CYS186 4.1 13.8 1.0
NH1 B:DP1791 4.2 47.3 0.3
NH1 B:DP1791 4.3 18.6 0.7
C3D B:HEM700 4.3 18.0 1.0
C3A B:HEM700 4.3 15.3 1.0
C2D B:HEM700 4.3 16.0 1.0
C2B B:HEM700 4.3 17.0 1.0
C2A B:HEM700 4.3 16.3 1.0
NE1 B:TRP180 4.3 15.2 1.0
C3B B:HEM700 4.3 16.6 1.0
C3C B:HEM700 4.3 15.0 1.0
C2C B:HEM700 4.4 15.0 1.0
NO B:DP1791 4.4 20.3 0.7
NO B:DP1791 4.5 47.5 0.3
O2 B:DP1791 4.6 47.4 0.3
CZ B:DP1791 4.6 19.2 0.7
O2 B:DP1791 4.7 19.5 0.7
CZ B:DP1791 4.8 47.2 0.3
O3 B:DP1791 4.8 17.8 0.7
N B:GLY188 4.8 14.6 1.0
C B:CYS186 4.9 14.2 1.0
NH2 B:DP1791 4.9 46.6 0.3
NH2 B:DP1791 4.9 15.3 0.7
CD1 B:TRP180 5.0 14.7 1.0
N B:VAL187 5.0 13.4 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 14:28:56 2020

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