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Zinc in PDB 6l1x: Quinol-Dependent Nitric Oxide Reductase (Qnor) From Neisseria Meningitidis in the Monomeric Oxidized State with Zinc Complex.

Enzymatic activity of Quinol-Dependent Nitric Oxide Reductase (Qnor) From Neisseria Meningitidis in the Monomeric Oxidized State with Zinc Complex.

All present enzymatic activity of Quinol-Dependent Nitric Oxide Reductase (Qnor) From Neisseria Meningitidis in the Monomeric Oxidized State with Zinc Complex.:
1.7.99.7;

Protein crystallography data

The structure of Quinol-Dependent Nitric Oxide Reductase (Qnor) From Neisseria Meningitidis in the Monomeric Oxidized State with Zinc Complex., PDB code: 6l1x was solved by M.M.A.Jamali, S.V.Antonyuk, T.Tosha, K.Muramoto, S.S.Hasnain, Y.Shiro, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 49.92 / 3.15
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 96.120, 116.680, 123.550, 90.00, 90.00, 90.00
R / Rfree (%) 25 / 30.3

Other elements in 6l1x:

The structure of Quinol-Dependent Nitric Oxide Reductase (Qnor) From Neisseria Meningitidis in the Monomeric Oxidized State with Zinc Complex. also contains other interesting chemical elements:

Iron (Fe) 3 atoms
Calcium (Ca) 1 atom

Zinc Binding Sites:

The binding sites of Zinc atom in the Quinol-Dependent Nitric Oxide Reductase (Qnor) From Neisseria Meningitidis in the Monomeric Oxidized State with Zinc Complex. (pdb code 6l1x). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 3 binding sites of Zinc where determined in the Quinol-Dependent Nitric Oxide Reductase (Qnor) From Neisseria Meningitidis in the Monomeric Oxidized State with Zinc Complex., PDB code: 6l1x:
Jump to Zinc binding site number: 1; 2; 3;

Zinc binding site 1 out of 3 in 6l1x

Go back to Zinc Binding Sites List in 6l1x
Zinc binding site 1 out of 3 in the Quinol-Dependent Nitric Oxide Reductase (Qnor) From Neisseria Meningitidis in the Monomeric Oxidized State with Zinc Complex.


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Quinol-Dependent Nitric Oxide Reductase (Qnor) From Neisseria Meningitidis in the Monomeric Oxidized State with Zinc Complex. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn805

b:0.5
occ:1.00
 NE2 A:HIS577 2.0 91.1 1.0
OE1 A:GLU576 2.1 89.5 1.0
OE1 A:GLU573 2.1 0.7 1.0
ND1 A:HIS257 2.2 1.0 1.0
CD2 A:HIS577 2.7 97.1 1.0
CD A:GLU576 2.9 82.7 1.0
CE1 A:HIS577 3.0 82.8 1.0
OE2 A:GLU576 3.0 77.6 1.0
CE1 A:HIS257 3.1 0.5 1.0
CD A:GLU573 3.2 0.8 1.0
CG A:HIS257 3.2 0.8 1.0
CB A:HIS257 3.5 0.2 1.0
OE2 A:GLU573 3.7 0.5 1.0
CG A:HIS577 3.7 97.6 1.0
ND1 A:HIS577 3.8 87.4 1.0
NE2 A:HIS257 4.2 0.0 1.0
CD2 A:HIS257 4.3 0.5 1.0
CG A:GLU576 4.3 90.1 1.0
CG A:GLU573 4.4 0.9 1.0
CB A:GLU573 4.6 0.5 1.0
CB A:GLU576 4.8 99.9 1.0
CA A:GLU573 4.9 0.3 1.0
CA A:HIS257 4.9 0.6 1.0
O A:GLU573 5.0 0.9 1.0
N A:HIS577 5.0 0.9 1.0

Zinc binding site 2 out of 3 in 6l1x

Go back to Zinc Binding Sites List in 6l1x
Zinc binding site 2 out of 3 in the Quinol-Dependent Nitric Oxide Reductase (Qnor) From Neisseria Meningitidis in the Monomeric Oxidized State with Zinc Complex.


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Quinol-Dependent Nitric Oxide Reductase (Qnor) From Neisseria Meningitidis in the Monomeric Oxidized State with Zinc Complex. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn806

b:0.0
occ:1.00
 OE1 A:GLN713 2.1 0.8 1.0
NE2 A:HIS172 2.1 0.1 1.0
CD2 A:HIS172 3.1 0.8 1.0
CE1 A:HIS172 3.1 0.3 1.0
CD A:GLN713 3.3 0.2 1.0
ND1 A:HIS172 4.1 0.0 1.0
CG A:HIS172 4.1 0.2 1.0
NE2 A:GLN713 4.2 0.4 1.0
CG A:GLN713 4.4 0.8 1.0
CB A:GLN713 4.9 0.0 1.0

Zinc binding site 3 out of 3 in 6l1x

Go back to Zinc Binding Sites List in 6l1x
Zinc binding site 3 out of 3 in the Quinol-Dependent Nitric Oxide Reductase (Qnor) From Neisseria Meningitidis in the Monomeric Oxidized State with Zinc Complex.


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Quinol-Dependent Nitric Oxide Reductase (Qnor) From Neisseria Meningitidis in the Monomeric Oxidized State with Zinc Complex. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn807

b:0.8
occ:1.00
 OE2 A:GLU494 2.1 0.5 1.0
OE1 A:GLU563 2.1 0.7 1.0
OE2 A:GLU498 2.1 0.7 1.0
OE2 A:GLU563 2.1 0.8 1.0
OE1 A:GLU494 2.1 0.2 1.0
OE1 A:GLU498 2.1 0.1 1.0
CD A:GLU563 2.3 0.8 1.0
CD A:GLU494 2.4 1.0 1.0
CD A:GLU498 2.4 0.9 1.0
CG A:GLU563 3.8 0.9 1.0
CG A:GLU494 3.9 0.2 1.0
CG A:GLU498 3.9 0.1 1.0
CD1 A:PHE531 4.1 78.9 1.0
O A:PHE531 4.5 94.4 1.0
CE1 A:PHE531 4.6 79.5 1.0
CBB A:HEM802 4.6 0.3 1.0
O A:GLU494 4.7 0.2 1.0
CB A:GLU494 4.8 0.1 1.0
CB A:GLU563 4.8 0.3 1.0
CB A:GLU498 4.8 0.5 1.0
OH A:TYR642 4.9 98.8 1.0
C A:GLU494 5.0 0.6 1.0

Reference:

M.M.A.Jamali, C.C.Gopalasingam, R.M.Johnson, T.Tosha, K.Muramoto, S.P.Muench, S.V.Antonyuk, Y.Shiro, S.S.Hasnain. The Active Form of Quinol-Dependent Nitric Oxide Reductase From Neisseria Meningitidis Is A Dimer Iucrj V. 7 2020.
ISSN: ESSN 2052-2525
DOI: 10.1107/S2052252520003656
Page generated: Tue Oct 29 02:20:45 2024

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