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Zinc 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
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-(4R)- Amino-L-Proline Amide Bound (pdb code 1p6n). 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-(4R)- Amino-L-Proline Amide Bound, PDB code: 1p6n:

Zinc binding site 1 out of 1 in 1p6n

Go back to Zinc Binding Sites List in 1p6n
Zinc binding site 1 out of 1 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 Zinc with other atoms in the Zn 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
B:Zn900

b:50.0
occ:1.00
 SG B:CYS101 2.3 56.9 1.0
SG A:CYS101 2.3 49.2 1.0
SG B:CYS96 2.3 54.7 1.0
SG A:CYS96 2.3 55.3 1.0
CB B:CYS101 3.3 59.0 1.0
CB A:CYS101 3.4 55.5 1.0
CB B:CYS96 3.5 59.3 1.0
CB A:CYS96 3.6 57.6 1.0
CA B:CYS101 3.8 59.4 1.0
CA A:CYS101 3.8 56.8 1.0
N A:GLY103 4.0 55.9 1.0
N B:GLY103 4.1 57.7 1.0
N B:LEU102 4.2 59.9 1.0
CA A:GLY103 4.2 55.1 1.0
N A:LEU102 4.3 56.2 1.0
C A:CYS101 4.4 56.8 1.0
C B:CYS101 4.4 58.8 1.0
CA B:GLY103 4.4 57.7 1.0
CA B:CYS96 4.9 59.3 1.0
CA A:CYS96 5.0 59.4 1.0
C A:LEU102 5.0 56.8 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: Wed Oct 16 17:45:34 2024

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