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Zinc in PDB 1d0c: Bovine Endothelial Nitric Oxide Synthase Heme Domain Complexed with 3- Bromo-7-Nitroindazole (H4B Free)

Enzymatic activity of Bovine Endothelial Nitric Oxide Synthase Heme Domain Complexed with 3- Bromo-7-Nitroindazole (H4B Free)

All present enzymatic activity of Bovine Endothelial Nitric Oxide Synthase Heme Domain Complexed with 3- Bromo-7-Nitroindazole (H4B Free):
1.14.13.39;

Protein crystallography data

The structure of Bovine Endothelial Nitric Oxide Synthase Heme Domain Complexed with 3- Bromo-7-Nitroindazole (H4B Free), PDB code: 1d0c 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) 8.00 / 1.65
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 57.440, 105.980, 155.790, 90.00, 90.00, 90.00
R / Rfree (%) 21.3 / 25.9

Other elements in 1d0c:

The structure of Bovine Endothelial Nitric Oxide Synthase Heme Domain Complexed with 3- Bromo-7-Nitroindazole (H4B Free) also contains other interesting chemical elements:

Bromine (Br) 4 atoms
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 3- Bromo-7-Nitroindazole (H4B Free) (pdb code 1d0c). 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 3- Bromo-7-Nitroindazole (H4B Free), PDB code: 1d0c:

Zinc binding site 1 out of 1 in 1d0c

Go back to Zinc Binding Sites List in 1d0c
Zinc binding site 1 out of 1 in the Bovine Endothelial Nitric Oxide Synthase Heme Domain Complexed with 3- Bromo-7-Nitroindazole (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 3- Bromo-7-Nitroindazole (H4B Free) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn900

b:26.2
occ:1.00
 SG B:CYS96 2.3 28.0 1.0
SG A:CYS101 2.3 30.0 1.0
SG B:CYS101 2.4 30.8 1.0
SG A:CYS96 2.4 30.7 1.0
CB B:CYS101 3.2 26.2 1.0
CB A:CYS101 3.2 27.0 1.0
CB B:CYS96 3.4 24.6 1.0
CB A:CYS96 3.4 31.3 1.0
CA B:CYS101 3.7 26.5 1.0
CA A:CYS101 3.7 26.2 1.0
N B:GLY103 4.1 28.7 1.0
N A:GLY103 4.2 28.0 1.0
N B:LEU102 4.2 30.7 1.0
N A:LEU102 4.3 27.6 1.0
C B:CYS101 4.3 30.8 1.0
C A:CYS101 4.4 33.3 1.0
CA A:GLY103 4.4 33.3 1.0
CA B:GLY103 4.5 27.4 1.0
O B:HOH1093 4.5 47.1 1.0
CA B:CYS96 4.7 28.5 1.0
CA A:CYS96 4.8 40.2 1.0
O A:HOH1143 4.8 40.5 1.0
O A:HOH1099 4.8 42.3 1.0
N A:CYS101 5.0 29.5 1.0
N B:CYS101 5.0 31.3 1.0

Reference:

C.S.Raman, H.Li, P.Martasek, G.Southan, B.S.Masters, T.L.Poulos. Crystal Structure of Nitric Oxide Synthase Bound to Nitro Indazole Reveals A Novel Inactivation Mechanism. Biochemistry V. 40 13448 2001.
ISSN: ISSN 0006-2960
PubMed: 11695891
DOI: 10.1021/BI010957U
Page generated: Sat Oct 12 23:24:05 2024

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