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Zinc in PDB 1p6l: Bovine Endothelial Nos Heme Domain with L-N(Omega)-Nitroarginine-2,4- L-Diaminobutyric Amide Bound

Enzymatic activity of Bovine Endothelial Nos Heme Domain with L-N(Omega)-Nitroarginine-2,4- L-Diaminobutyric Amide Bound

All present enzymatic activity of Bovine Endothelial Nos Heme Domain with L-N(Omega)-Nitroarginine-2,4- L-Diaminobutyric Amide Bound:
1.14.13.39;

Protein crystallography data

The structure of Bovine Endothelial Nos Heme Domain with L-N(Omega)-Nitroarginine-2,4- L-Diaminobutyric Amide Bound, PDB code: 1p6l 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) 34.98 / 2.35
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 57.773, 106.243, 156.487, 90.00, 90.00, 90.00
R / Rfree (%) 21.4 / 27.2

Other elements in 1p6l:

The structure of Bovine Endothelial Nos Heme Domain with L-N(Omega)-Nitroarginine-2,4- L-Diaminobutyric Amide Bound also contains other interesting chemical elements:

Arsenic (As) 2 atoms
Iron (Fe) 2 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Bovine Endothelial Nos Heme Domain with L-N(Omega)-Nitroarginine-2,4- L-Diaminobutyric Amide Bound (pdb code 1p6l). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Bovine Endothelial Nos Heme Domain with L-N(Omega)-Nitroarginine-2,4- L-Diaminobutyric Amide Bound, PDB code: 1p6l:

Zinc binding site 1 out of 1 in 1p6l

Go back to Zinc Binding Sites List in 1p6l
Zinc binding site 1 out of 1 in the Bovine Endothelial Nos Heme Domain with L-N(Omega)-Nitroarginine-2,4- L-Diaminobutyric Amide Bound


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Bovine Endothelial Nos Heme Domain with L-N(Omega)-Nitroarginine-2,4- L-Diaminobutyric Amide Bound within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn900

b:36.3
occ:1.00
 SG A:CYS101 2.3 35.9 1.0
SG B:CYS101 2.3 37.4 1.0
SG B:CYS96 2.3 36.9 1.0
SG A:CYS96 2.3 39.0 1.0
CB B:CYS101 3.1 41.2 1.0
CB A:CYS101 3.3 36.8 1.0
CB B:CYS96 3.4 41.0 1.0
CB A:CYS96 3.6 42.5 1.0
CA B:CYS101 3.6 40.6 1.0
CA A:CYS101 3.7 37.6 1.0
N A:GLY103 4.0 37.3 1.0
N B:GLY103 4.1 39.0 1.0
N B:LEU102 4.2 40.1 1.0
N A:LEU102 4.2 36.6 1.0
CA A:GLY103 4.3 37.2 1.0
C A:CYS101 4.3 37.1 1.0
C B:CYS101 4.3 40.4 1.0
CA B:GLY103 4.5 38.4 1.0
CA B:CYS96 4.8 41.5 1.0
O A:HOH993 4.9 37.0 1.0
N B:CYS101 4.9 41.4 1.0
CA A:CYS96 4.9 44.3 1.0
O B:HOH985 4.9 37.8 1.0
N A:CYS101 5.0 39.1 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: Mon Jan 25 16:11:18 2021

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