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Zinc in PDB 3nos: Human Endothelial Nitric Oxide Synthase with Arginine Substrate

Enzymatic activity of Human Endothelial Nitric Oxide Synthase with Arginine Substrate

All present enzymatic activity of Human Endothelial Nitric Oxide Synthase with Arginine Substrate:
1.14.13.39;

Protein crystallography data

The structure of Human Endothelial Nitric Oxide Synthase with Arginine Substrate, PDB code: 3nos was solved by T.O.Fischmann, P.C.Weber, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 8.00 / 2.40
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 68.859, 93.264, 156.117, 90.00, 90.00, 90.00
R / Rfree (%) 19.3 / 30.8

Other elements in 3nos:

The structure of Human Endothelial Nitric Oxide Synthase with Arginine Substrate also contains other interesting chemical elements:

Iron (Fe) 2 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Human Endothelial Nitric Oxide Synthase with Arginine Substrate (pdb code 3nos). 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 Human Endothelial Nitric Oxide Synthase with Arginine Substrate, PDB code: 3nos:

Zinc binding site 1 out of 1 in 3nos

Go back to Zinc Binding Sites List in 3nos
Zinc binding site 1 out of 1 in the Human Endothelial Nitric Oxide Synthase with Arginine Substrate


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Human Endothelial Nitric Oxide Synthase with Arginine Substrate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn1000

b:23.3
occ:1.00
SG A:CYS94 2.2 15.1 1.0
SG B:CYS94 2.2 20.3 1.0
SG A:CYS99 2.4 26.0 1.0
SG B:CYS99 2.5 25.6 1.0
CB B:CYS99 3.1 19.3 1.0
CB B:CYS94 3.2 15.5 1.0
CB A:CYS99 3.3 19.1 1.0
CB A:CYS94 3.4 17.4 1.0
CA B:CYS99 3.6 17.6 1.0
CA A:CYS99 3.8 20.0 1.0
N B:LEU100 4.2 19.8 1.0
N B:GLY101 4.2 16.2 1.0
C B:CYS99 4.2 20.6 1.0
N A:GLY101 4.3 21.7 1.0
N A:LEU100 4.4 20.6 1.0
C A:CYS99 4.4 20.6 1.0
CA B:CYS94 4.6 20.5 1.0
CA B:GLY101 4.6 17.1 1.0
CA A:GLY101 4.6 21.2 1.0
CA A:CYS94 4.7 22.4 1.0
N B:CYS99 4.9 20.6 1.0

Reference:

T.O.Fischmann, A.Hruza, X.D.Niu, J.D.Fossetta, C.A.Lunn, E.Dolphin, A.J.Prongay, P.Reichert, D.J.Lundell, S.K.Narula, P.C.Weber. Structural Characterization of Nitric Oxide Synthase Isoforms Reveals Striking Active-Site Conservation. Nat.Struct.Biol. V. 6 233 1999.
ISSN: ISSN 1072-8368
PubMed: 10074942
DOI: 10.1038/6675
Page generated: Wed Dec 16 04:39:10 2020

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