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Calcium in PDB 6qq6: Cryo-Em Structure of Dimeric Quinol Dependent Nitric Oxide Reductase (Qnor) VAL495ALA Mutant From Alcaligenes Xylosoxidans

Enzymatic activity of Cryo-Em Structure of Dimeric Quinol Dependent Nitric Oxide Reductase (Qnor) VAL495ALA Mutant From Alcaligenes Xylosoxidans

All present enzymatic activity of Cryo-Em Structure of Dimeric Quinol Dependent Nitric Oxide Reductase (Qnor) VAL495ALA Mutant From Alcaligenes Xylosoxidans:
1.7.2.5;

Other elements in 6qq6:

The structure of Cryo-Em Structure of Dimeric Quinol Dependent Nitric Oxide Reductase (Qnor) VAL495ALA Mutant From Alcaligenes Xylosoxidans also contains other interesting chemical elements:

Iron (Fe) 6 atoms

Calcium Binding Sites:

The binding sites of Calcium atom in the Cryo-Em Structure of Dimeric Quinol Dependent Nitric Oxide Reductase (Qnor) VAL495ALA Mutant From Alcaligenes Xylosoxidans (pdb code 6qq6). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the Cryo-Em Structure of Dimeric Quinol Dependent Nitric Oxide Reductase (Qnor) VAL495ALA Mutant From Alcaligenes Xylosoxidans, PDB code: 6qq6:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in 6qq6

Go back to Calcium Binding Sites List in 6qq6
Calcium binding site 1 out of 2 in the Cryo-Em Structure of Dimeric Quinol Dependent Nitric Oxide Reductase (Qnor) VAL495ALA Mutant From Alcaligenes Xylosoxidans


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Cryo-Em Structure of Dimeric Quinol Dependent Nitric Oxide Reductase (Qnor) VAL495ALA Mutant From Alcaligenes Xylosoxidans within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca804

b:32.1
occ:1.00
O1A A:HEM802 2.1 43.4 1.0
OE2 A:GLU407 2.4 31.6 1.0
O1D A:HEM801 2.5 43.4 1.0
O2D A:HEM801 2.5 43.4 1.0
OH A:TYR78 2.7 38.2 1.0
O A:GLY76 2.8 26.3 1.0
CGD A:HEM801 2.8 43.4 1.0
CGA A:HEM802 2.9 43.4 1.0
OE1 A:GLU407 3.0 31.6 1.0
O2A A:HEM802 3.0 43.4 1.0
CD A:GLU407 3.1 31.6 1.0
CZ A:TYR78 3.5 38.2 1.0
CE2 A:TYR78 3.8 38.2 1.0
C A:GLY76 3.9 26.3 1.0
NH2 A:ARG328 4.0 43.4 1.0
N A:GLY76 4.1 26.3 1.0
CBA A:HEM802 4.3 43.4 1.0
CBD A:HEM801 4.3 43.4 1.0
OH A:TYR408 4.3 31.9 1.0
CA A:GLY76 4.5 26.3 1.0
CE1 A:TYR78 4.5 38.2 1.0
CAA A:HEM802 4.5 43.4 1.0
CG A:GLU407 4.6 31.6 1.0
CE2 A:TYR408 4.9 31.9 1.0
CAD A:HEM801 4.9 43.4 1.0
CD2 A:TYR78 5.0 38.2 1.0
N A:ALA77 5.0 29.0 1.0
CG2 A:THR626 5.0 26.0 1.0

Calcium binding site 2 out of 2 in 6qq6

Go back to Calcium Binding Sites List in 6qq6
Calcium binding site 2 out of 2 in the Cryo-Em Structure of Dimeric Quinol Dependent Nitric Oxide Reductase (Qnor) VAL495ALA Mutant From Alcaligenes Xylosoxidans


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Cryo-Em Structure of Dimeric Quinol Dependent Nitric Oxide Reductase (Qnor) VAL495ALA Mutant From Alcaligenes Xylosoxidans within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Ca804

b:31.3
occ:1.00
O1A B:HEM802 2.1 43.4 1.0
OE2 B:GLU407 2.4 32.0 1.0
O1D B:HEM801 2.5 43.4 1.0
O2D B:HEM801 2.5 43.4 1.0
OH B:TYR78 2.7 38.3 1.0
O B:GLY76 2.8 26.5 1.0
CGD B:HEM801 2.8 43.4 1.0
CGA B:HEM802 2.9 43.4 1.0
OE1 B:GLU407 3.0 32.0 1.0
O2A B:HEM802 3.0 43.4 1.0
CD B:GLU407 3.1 32.0 1.0
CZ B:TYR78 3.5 38.3 1.0
CE2 B:TYR78 3.8 38.3 1.0
C B:GLY76 3.9 26.5 1.0
NH2 B:ARG328 4.0 43.4 1.0
N B:GLY76 4.1 26.5 1.0
CBA B:HEM802 4.2 43.4 1.0
CBD B:HEM801 4.3 43.4 1.0
OH B:TYR408 4.3 35.3 1.0
CA B:GLY76 4.4 26.5 1.0
CE1 B:TYR78 4.5 38.3 1.0
CAA B:HEM802 4.5 43.4 1.0
CG B:GLU407 4.5 32.0 1.0
CE2 B:TYR408 4.8 35.3 1.0
CAD B:HEM801 4.9 43.4 1.0
CD2 B:TYR78 5.0 38.3 1.0
N B:ALA77 5.0 29.0 1.0

Reference:

C.C.Gopalasingam, R.M.Johnson, G.N.Chiduza, T.Tosha, M.Yamamoto, Y.Shiro, S.V.Antonyuk, S.P.Muench, S.S.Hasnain. Dimeric Structures of Quinol-Dependent Nitric Oxide Reductases (Qnors) Revealed By Cryo-Electron Microscopy. Sci Adv V. 5 X1803 2019.
ISSN: ESSN 2375-2548
PubMed: 31489376
DOI: 10.1126/SCIADV.AAX1803
Page generated: Tue Jul 16 14:00:58 2024

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