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Zinc in PDB 1d1w: Bovine Endothelial Nitric Oxide Synthase Heme Domain Complexed with 2- Aminothiazoline (H4B Bound)

Enzymatic activity of Bovine Endothelial Nitric Oxide Synthase Heme Domain Complexed with 2- Aminothiazoline (H4B Bound)

All present enzymatic activity of Bovine Endothelial Nitric Oxide Synthase Heme Domain Complexed with 2- Aminothiazoline (H4B Bound):
1.14.13.39;

Protein crystallography data

The structure of Bovine Endothelial Nitric Oxide Synthase Heme Domain Complexed with 2- Aminothiazoline (H4B Bound), PDB code: 1d1w was solved by H.Li, C.S.Raman, P.Martasek, V.Kral, B.S.S.Masters, T.L.Poulos, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 50.00 / 2.00
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 58.460, 106.320, 156.330, 90.00, 90.00, 90.00
R / Rfree (%) 20.4 / 25

Other elements in 1d1w:

The structure of Bovine Endothelial Nitric Oxide Synthase Heme Domain Complexed with 2- Aminothiazoline (H4B 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 Nitric Oxide Synthase Heme Domain Complexed with 2- Aminothiazoline (H4B Bound) (pdb code 1d1w). 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 Nitric Oxide Synthase Heme Domain Complexed with 2- Aminothiazoline (H4B Bound), PDB code: 1d1w:

Zinc binding site 1 out of 1 in 1d1w

Go back to Zinc Binding Sites List in 1d1w
Zinc binding site 1 out of 1 in the Bovine Endothelial Nitric Oxide Synthase Heme Domain Complexed with 2- Aminothiazoline (H4B 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 Nitric Oxide Synthase Heme Domain Complexed with 2- Aminothiazoline (H4B Bound) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn900

b:34.8
occ:1.00
 SG B:CYS96 2.3 35.6 1.0
SG A:CYS101 2.3 34.6 1.0
SG B:CYS101 2.3 33.7 1.0
SG A:CYS96 2.3 36.8 1.0
CB A:CYS101 3.2 36.2 1.0
CB B:CYS101 3.3 29.3 1.0
CB A:CYS96 3.4 35.1 1.0
CB B:CYS96 3.5 38.7 1.0
CA A:CYS101 3.7 41.4 1.0
CA B:CYS101 3.7 34.3 1.0
N B:GLY103 4.1 35.4 1.0
N A:GLY103 4.1 37.4 1.0
N B:LEU102 4.1 37.6 1.0
N A:LEU102 4.2 35.4 1.0
C A:CYS101 4.3 36.4 1.0
C B:CYS101 4.3 37.3 1.0
CA B:GLY103 4.4 33.1 1.0
CA A:GLY103 4.5 37.9 1.0
O A:HOH1139 4.8 43.6 1.0
CA A:CYS96 4.8 40.3 1.0
CA B:CYS96 4.8 38.8 1.0
N A:CYS101 5.0 42.5 1.0

Reference:

H.Li, C.S.Raman, P.Martasek, V.Kral, B.S.Masters, T.L.Poulos. Mapping the Active Site Polarity in Structures of Endothelial Nitric Oxide Synthase Heme Domain Complexed with Isothioureas. J.Inorg.Biochem. V. 81 133 2000.
ISSN: ISSN 0162-0134
PubMed: 11051558
DOI: 10.1016/S0162-0134(00)00099-4
Page generated: Sat Oct 12 23:27:00 2024

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