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Zinc in PDB 1d1y: Bovine Endothelial Nitric Oxide Synthase Heme Domain Complexed with 1, 3-Pbitu (H4B Free)

Enzymatic activity of Bovine Endothelial Nitric Oxide Synthase Heme Domain Complexed with 1, 3-Pbitu (H4B Free)

All present enzymatic activity of Bovine Endothelial Nitric Oxide Synthase Heme Domain Complexed with 1, 3-Pbitu (H4B Free):
1.14.13.39;

Protein crystallography data

The structure of Bovine Endothelial Nitric Oxide Synthase Heme Domain Complexed with 1, 3-Pbitu (H4B Free), PDB code: 1d1y 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) 30.32 / 2.20
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 58.660, 106.250, 156.440, 90.00, 90.00, 90.00
R / Rfree (%) 22.3 / 26.8

Other elements in 1d1y:

The structure of Bovine Endothelial Nitric Oxide Synthase Heme Domain Complexed with 1, 3-Pbitu (H4B Free) 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, 3-Pbitu (H4B Free) (pdb code 1d1y). 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, 3-Pbitu (H4B Free), PDB code: 1d1y:

Zinc binding site 1 out of 1 in 1d1y

Go back to Zinc Binding Sites List in 1d1y
Zinc binding site 1 out of 1 in the Bovine Endothelial Nitric Oxide Synthase Heme Domain Complexed with 1, 3-Pbitu (H4B Free)


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, 3-Pbitu (H4B Free) within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn900

b:56.4
occ:1.00
 SG A:CYS101 2.3 59.2 1.0
SG B:CYS96 2.3 60.0 1.0
SG B:CYS101 2.3 58.6 1.0
SG A:CYS96 2.3 60.9 1.0
CB A:CYS101 3.2 63.5 1.0
CB B:CYS101 3.3 58.3 1.0
CB B:CYS96 3.5 63.1 1.0
CB A:CYS96 3.5 64.4 1.0
CA A:CYS101 3.7 64.3 1.0
CA B:CYS101 3.8 59.1 1.0
N B:GLY103 4.2 58.1 1.0
N A:GLY103 4.2 61.6 1.0
C A:CYS101 4.3 63.6 1.0
N A:LEU102 4.3 63.0 1.0
N B:LEU102 4.4 59.3 1.0
C B:CYS101 4.4 59.4 1.0
CA B:GLY103 4.5 58.2 1.0
CA A:GLY103 4.5 60.9 1.0
CA B:CYS96 4.7 63.3 1.0
CA A:CYS96 4.8 65.9 1.0
N A:CYS101 5.0 65.8 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 23:27:35 2024

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