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Zinc in PDB 1d1x: Bovine Endothelial Nitric Oxide Synthase Heme Domain Complexed with 1, 4-Pbitu (H4B Bound)

Enzymatic activity of Bovine Endothelial Nitric Oxide Synthase Heme Domain Complexed with 1, 4-Pbitu (H4B Bound)

All present enzymatic activity of Bovine Endothelial Nitric Oxide Synthase Heme Domain Complexed with 1, 4-Pbitu (H4B Bound):
1.14.13.39;

Protein crystallography data

The structure of Bovine Endothelial Nitric Oxide Synthase Heme Domain Complexed with 1, 4-Pbitu (H4B Bound), PDB code: 1d1x was solved by C.S.Raman, H.Li, P.Martasek, G.J.Southan, 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) 36.61 / 2.00
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 58.530, 106.730, 156.730, 90.00, 90.00, 90.00
R / Rfree (%) 22 / 25.4

Other elements in 1d1x:

The structure of Bovine Endothelial Nitric Oxide Synthase Heme Domain Complexed with 1, 4-Pbitu (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 1, 4-Pbitu (H4B Bound) (pdb code 1d1x). 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 1, 4-Pbitu (H4B Bound), PDB code: 1d1x:

Zinc binding site 1 out of 1 in 1d1x

Go back to Zinc Binding Sites List in 1d1x
Zinc binding site 1 out of 1 in the Bovine Endothelial Nitric Oxide Synthase Heme Domain Complexed with 1, 4-Pbitu (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 1, 4-Pbitu (H4B Bound) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn901

b:38.4
occ:1.00
 SG B:CYS96 2.3 38.5 1.0
SG B:CYS101 2.3 38.0 1.0
SG A:CYS101 2.3 37.7 1.0
SG A:CYS96 2.3 40.0 1.0
CB B:CYS101 3.2 38.0 1.0
CB A:CYS101 3.4 41.1 1.0
CB A:CYS96 3.4 41.7 1.0
CB B:CYS96 3.5 41.1 1.0
CA B:CYS101 3.7 39.1 1.0
CA A:CYS101 3.8 43.2 1.0
N B:GLY103 4.1 40.6 1.0
N A:GLY103 4.1 38.2 1.0
N B:LEU102 4.1 39.2 1.0
N A:LEU102 4.2 41.2 1.0
C B:CYS101 4.3 39.1 1.0
C A:CYS101 4.4 42.2 1.0
CA A:GLY103 4.4 38.8 1.0
CA B:GLY103 4.5 40.1 1.0
CA A:CYS96 4.8 43.5 1.0
CA B:CYS96 4.9 41.5 1.0

Reference:

C.S.Raman, H.Li, P.Martasek, B.R.Babu, O.W.Griffith, B.S.Masters, T.L.Poulos. Implications For Isoform-Selective Inhibitor Design Derived From the Binding Mode of Bulky Isothioureas to the Heme Domain of Endothelial Nitric-Oxide Synthase. J.Biol.Chem. V. 276 26486 2001.
ISSN: ISSN 0021-9258
PubMed: 11331290
DOI: 10.1074/JBC.M102255200
Page generated: Sat Oct 12 23:27:36 2024

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