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Sodium in PDB 8rpl: Amp-Forming Acetyl-Coa Synthetase From Chloroflexota Bacterium with Bound Acetyl Amp

Enzymatic activity of Amp-Forming Acetyl-Coa Synthetase From Chloroflexota Bacterium with Bound Acetyl Amp

All present enzymatic activity of Amp-Forming Acetyl-Coa Synthetase From Chloroflexota Bacterium with Bound Acetyl Amp:
6.2.1.1;

Protein crystallography data

The structure of Amp-Forming Acetyl-Coa Synthetase From Chloroflexota Bacterium with Bound Acetyl Amp, PDB code: 8rpl was solved by K.Striska, G.J.Palm, M.Lammers, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 48.30 / 2.37
Space group H 3 2
Cell size a, b, c (Å), α, β, γ (°) 161.909, 161.909, 817.234, 90, 90, 120
R / Rfree (%) 16.1 / 20.1

Other elements in 8rpl:

The structure of Amp-Forming Acetyl-Coa Synthetase From Chloroflexota Bacterium with Bound Acetyl Amp also contains other interesting chemical elements:

Magnesium (Mg) 3 atoms

Sodium Binding Sites:

The binding sites of Sodium atom in the Amp-Forming Acetyl-Coa Synthetase From Chloroflexota Bacterium with Bound Acetyl Amp (pdb code 8rpl). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total only one binding site of Sodium was determined in the Amp-Forming Acetyl-Coa Synthetase From Chloroflexota Bacterium with Bound Acetyl Amp, PDB code: 8rpl:

Sodium binding site 1 out of 1 in 8rpl

Go back to Sodium Binding Sites List in 8rpl
Sodium binding site 1 out of 1 in the Amp-Forming Acetyl-Coa Synthetase From Chloroflexota Bacterium with Bound Acetyl Amp


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Amp-Forming Acetyl-Coa Synthetase From Chloroflexota Bacterium with Bound Acetyl Amp within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Na703

b:76.6
occ:1.00
O D:HOH811 2.1 84.8 1.0
O D:VAL552 2.4 71.8 1.0
O D:VAL557 2.6 73.2 1.0
O D:HIS554 2.7 80.6 1.0
HE D:ARG581 3.5 101.1 1.0
HH22 D:ARG581 3.5 101.8 1.0
C D:VAL552 3.6 77.0 1.0
HG11 D:VAL552 3.7 73.5 1.0
C D:HIS554 3.8 78.6 1.0
C D:VAL557 3.8 72.1 1.0
HA D:PRO555 3.9 84.8 1.0
H D:VAL557 3.9 73.2 1.0
HB D:VAL557 3.9 75.4 1.0
NH2 D:ARG581 4.1 102.1 1.0
HA D:VAL552 4.1 75.1 1.0
HG12 D:VAL552 4.2 73.5 1.0
NE D:ARG581 4.2 103.9 1.0
HA D:ALA558 4.3 76.5 1.0
HA D:SER553 4.3 82.1 1.0
C D:SER553 4.3 84.5 1.0
CG1 D:VAL552 4.4 72.4 1.0
N D:HIS554 4.4 81.4 1.0
N D:VAL557 4.4 72.6 1.0
CA D:PRO555 4.4 83.9 1.0
CA D:VAL552 4.4 74.4 1.0
N D:PRO555 4.5 85.6 1.0
HH21 D:ARG581 4.5 102.2 1.0
CA D:VAL557 4.5 72.9 1.0
N D:SER553 4.5 80.1 1.0
C D:PRO555 4.5 81.8 1.0
H D:HIS554 4.6 80.6 1.0
O D:SER553 4.6 94.5 1.0
CZ D:ARG581 4.6 102.3 1.0
CA D:SER553 4.6 81.1 1.0
O D:PRO555 4.7 83.5 1.0
CB D:VAL557 4.7 75.2 1.0
CA D:HIS554 4.7 77.7 1.0
N D:ALA558 4.8 73.7 1.0
CA D:ALA558 5.0 76.1 1.0

Reference:

C.Qin, M.Lammers. The Amp-Forming Acetyl-Coa-Synthetase Is Regulated By Lysine Acetylation and Has An Intrinsic Phosphotransacetylase Activity to Adjust Its Activity to the Cellular Acetyl-Phosphate Level Nature Comm 2024.
Page generated: Wed Oct 9 13:22:17 2024

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