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Iron in PDB 6t6v: Glu-494-Ala Inactive Monomer of A Quinol Dependent Nitric Oxide Reductase (Qnor) From Alcaligenes Xylosoxidans

Enzymatic activity of Glu-494-Ala Inactive Monomer of A Quinol Dependent Nitric Oxide Reductase (Qnor) From Alcaligenes Xylosoxidans

All present enzymatic activity of Glu-494-Ala Inactive Monomer of A Quinol Dependent Nitric Oxide Reductase (Qnor) From Alcaligenes Xylosoxidans:
1.7.2.5;

Other elements in 6t6v:

The structure of Glu-494-Ala Inactive Monomer of A Quinol Dependent Nitric Oxide Reductase (Qnor) From Alcaligenes Xylosoxidans also contains other interesting chemical elements:

Calcium (Ca) 1 atom

Iron Binding Sites:

The binding sites of Iron atom in the Glu-494-Ala Inactive Monomer of A Quinol Dependent Nitric Oxide Reductase (Qnor) From Alcaligenes Xylosoxidans (pdb code 6t6v). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Glu-494-Ala Inactive Monomer of A Quinol Dependent Nitric Oxide Reductase (Qnor) From Alcaligenes Xylosoxidans, PDB code: 6t6v:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in 6t6v

Go back to Iron Binding Sites List in 6t6v
Iron binding site 1 out of 2 in the Glu-494-Ala Inactive Monomer of A Quinol Dependent Nitric Oxide Reductase (Qnor) From Alcaligenes Xylosoxidans


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Glu-494-Ala Inactive Monomer of A Quinol Dependent Nitric Oxide Reductase (Qnor) From Alcaligenes Xylosoxidans within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe801

b:94.7
occ:1.00
FE A:HEM801 0.0 94.7 1.0
ND A:HEM801 1.9 94.7 1.0
NA A:HEM801 2.0 94.7 1.0
NE2 A:HIS631 2.0 95.5 1.0
NC A:HEM801 2.1 94.7 1.0
NB A:HEM801 2.1 94.7 1.0
NE2 A:HIS331 2.1 92.6 1.0
C4D A:HEM801 2.9 94.7 1.0
C1D A:HEM801 2.9 94.7 1.0
CD2 A:HIS631 2.9 95.5 1.0
C1A A:HEM801 2.9 94.7 1.0
CE1 A:HIS331 3.0 92.6 1.0
C4C A:HEM801 3.0 94.7 1.0
C4A A:HEM801 3.0 94.7 1.0
C1B A:HEM801 3.1 94.7 1.0
C4B A:HEM801 3.1 94.7 1.0
CE1 A:HIS631 3.1 95.5 1.0
C1C A:HEM801 3.1 94.7 1.0
CD2 A:HIS331 3.2 92.6 1.0
CHA A:HEM801 3.3 94.7 1.0
CHD A:HEM801 3.3 94.7 1.0
CHB A:HEM801 3.5 94.7 1.0
CHC A:HEM801 3.5 94.7 1.0
CG A:HIS631 4.1 95.5 1.0
C3D A:HEM801 4.1 94.7 1.0
C2D A:HEM801 4.1 94.7 1.0
ND1 A:HIS631 4.1 95.5 1.0
C2A A:HEM801 4.1 94.7 1.0
ND1 A:HIS331 4.1 92.6 1.0
C3A A:HEM801 4.2 94.7 1.0
C3C A:HEM801 4.2 94.7 1.0
C2C A:HEM801 4.3 94.7 1.0
CG A:HIS331 4.3 92.6 1.0
C2B A:HEM801 4.3 94.7 1.0
C3B A:HEM801 4.3 94.7 1.0
NE2 A:GLN296 4.8 0.0 1.0

Iron binding site 2 out of 2 in 6t6v

Go back to Iron Binding Sites List in 6t6v
Iron binding site 2 out of 2 in the Glu-494-Ala Inactive Monomer of A Quinol Dependent Nitric Oxide Reductase (Qnor) From Alcaligenes Xylosoxidans


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Glu-494-Ala Inactive Monomer of A Quinol Dependent Nitric Oxide Reductase (Qnor) From Alcaligenes Xylosoxidans within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe802

b:92.8
occ:1.00
FE A:HEM802 0.0 92.8 1.0
ND A:HEM802 1.9 92.8 1.0
NA A:HEM802 2.0 92.8 1.0
NE2 A:HIS629 2.0 96.0 1.0
NC A:HEM802 2.1 92.8 1.0
NB A:HEM802 2.1 92.8 1.0
C4D A:HEM802 2.9 92.8 1.0
C1D A:HEM802 2.9 92.8 1.0
CE1 A:HIS629 2.9 96.0 1.0
C1A A:HEM802 2.9 92.8 1.0
CD2 A:HIS629 3.0 96.0 1.0
C4C A:HEM802 3.0 92.8 1.0
C4A A:HEM802 3.0 92.8 1.0
C1B A:HEM802 3.1 92.8 1.0
C4B A:HEM802 3.1 92.8 1.0
C1C A:HEM802 3.1 92.8 1.0
CHA A:HEM802 3.3 92.8 1.0
CHD A:HEM802 3.4 92.8 1.0
CHB A:HEM802 3.5 92.8 1.0
CHC A:HEM802 3.5 92.8 1.0
ND1 A:HIS629 4.1 96.0 1.0
C3D A:HEM802 4.1 92.8 1.0
C2D A:HEM802 4.1 92.8 1.0
CG A:HIS629 4.1 96.0 1.0
C2A A:HEM802 4.1 92.8 1.0
C3A A:HEM802 4.2 92.8 1.0
C3C A:HEM802 4.2 92.8 1.0
C2C A:HEM802 4.3 92.8 1.0
C2B A:HEM802 4.3 92.8 1.0
C3B A:HEM802 4.3 92.8 1.0

Reference:

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 2020.
ISSN: ESSN 2052-2525
DOI: 10.1107/S2052252520003656
Page generated: Wed Aug 7 10:38:05 2024

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