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Titanium in PDB 7nys: Monomeric Acetyl-Coa Synthase in Closed Conformation with Carbon Monoxide Bound to the Ni Proximal of Cluster A

Enzymatic activity of Monomeric Acetyl-Coa Synthase in Closed Conformation with Carbon Monoxide Bound to the Ni Proximal of Cluster A

All present enzymatic activity of Monomeric Acetyl-Coa Synthase in Closed Conformation with Carbon Monoxide Bound to the Ni Proximal of Cluster A:
2.3.1.169;

Protein crystallography data

The structure of Monomeric Acetyl-Coa Synthase in Closed Conformation with Carbon Monoxide Bound to the Ni Proximal of Cluster A, PDB code: 7nys was solved by J.Kreibich, J.H.Jeoung, H.Dobbek, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 48.56 / 2.00
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 70.276, 99.2, 238.584, 90, 90, 90
R / Rfree (%) 18.4 / 22.1

Other elements in 7nys:

The structure of Monomeric Acetyl-Coa Synthase in Closed Conformation with Carbon Monoxide Bound to the Ni Proximal of Cluster A also contains other interesting chemical elements:

Nickel (Ni) 4 atoms
Iron (Fe) 8 atoms
Chlorine (Cl) 2 atoms

Titanium Binding Sites:

The binding sites of Titanium atom in the Monomeric Acetyl-Coa Synthase in Closed Conformation with Carbon Monoxide Bound to the Ni Proximal of Cluster A (pdb code 7nys). This binding sites where shown within 5.0 Angstroms radius around Titanium atom.
In total only one binding site of Titanium was determined in the Monomeric Acetyl-Coa Synthase in Closed Conformation with Carbon Monoxide Bound to the Ni Proximal of Cluster A, PDB code: 7nys:

Titanium binding site 1 out of 1 in 7nys

Go back to Titanium Binding Sites List in 7nys
Titanium binding site 1 out of 1 in the Monomeric Acetyl-Coa Synthase in Closed Conformation with Carbon Monoxide Bound to the Ni Proximal of Cluster A


Mono view


Stereo pair view

A full contact list of Titanium with other atoms in the Ti binding site number 1 of Monomeric Acetyl-Coa Synthase in Closed Conformation with Carbon Monoxide Bound to the Ni Proximal of Cluster A within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Ti804

b:83.9
occ:1.00
TI1 B:UW8804 0.0 83.9 1.0
O9 B:UW8804 1.8 83.9 1.0
O2 B:UW8804 1.9 92.4 1.0
O16 B:UW8804 1.9 76.6 1.0
O1 B:UW8804 2.0 99.9 1.0
O8 B:UW8804 2.1 96.3 1.0
O15 B:UW8804 2.1 86.2 1.0
HZ2 A:LYS49 2.8 95.4 1.0
C8 B:UW8804 2.9 86.3 1.0
C2 B:UW8804 2.9 86.2 1.0
HZ1 B:LYS49 2.9 84.6 1.0
C7 B:UW8804 2.9 90.3 1.0
C1 B:UW8804 2.9 81.5 1.0
HZ2 B:LYS49 2.9 84.6 1.0
HZ1 A:LYS49 2.9 95.4 1.0
C14 B:UW8804 2.9 80.0 1.0
C13 B:UW8804 3.0 83.2 1.0
HZ3 A:LYS49 3.1 95.4 1.0
NZ A:LYS49 3.1 79.5 1.0
NZ B:LYS49 3.3 70.5 1.0
H11A B:UW8804 3.3 98.8 1.0
H5A B:UW8804 3.4 102.6 1.0
HZ1 B:LYS123 3.4 90.6 1.0
O18' B:UW8804 3.6 70.6 1.0
O11 B:UW8804 3.6 97.7 1.0
C5 B:UW8804 3.6 85.5 1.0
C11 B:UW8804 3.7 82.3 1.0
HZ3 B:LYS49 3.7 84.6 1.0
C18 B:UW8804 3.7 96.6 1.0
O20 B:UW8804 3.7 104.8 1.0
C17 B:UW8804 3.9 81.2 1.0
O6 B:UW8804 3.9 85.5 1.0
HZ2 B:LYS123 4.0 90.6 1.0
O10 B:UW8804 4.0 87.3 1.0
C9 B:UW8804 4.1 87.1 1.0
O3 B:UW8804 4.1 86.2 1.0
C3 B:UW8804 4.1 85.6 1.0
C10 B:UW8804 4.1 93.0 1.0
NZ B:LYS123 4.1 75.5 1.0
C15 B:UW8804 4.1 73.9 1.0
O17 B:UW8804 4.1 83.6 1.0
C6 B:UW8804 4.2 91.8 1.0
H17B B:UW8804 4.2 97.5 1.0
H3A B:UW8804 4.2 102.7 1.0
O21 B:UW8804 4.3 91.4 1.0
O5 B:UW8804 4.3 95.2 1.0
H9B B:UW8804 4.4 104.6 1.0
O14 B:UW8804 4.5 88.5 1.0
H15A B:UW8804 4.5 88.7 1.0
HE3 B:LYS49 4.5 67.2 1.0
H11B B:UW8804 4.5 98.8 1.0
C12 B:UW8804 4.5 86.9 1.0
CE B:LYS49 4.6 56.0 1.0
CE A:LYS49 4.6 63.9 1.0
C4 B:UW8804 4.6 98.6 1.0
H5B B:UW8804 4.6 102.6 1.0
C16' B:UW8804 4.6 69.2 1.0
HZ3 B:LYS123 4.7 90.6 1.0
HZ1 A:LYS123 4.7 92.0 1.0
HZ3 A:LYS123 4.7 92.0 1.0
HE3 B:LYS123 4.8 90.7 1.0
HE3 A:LYS49 4.9 76.7 1.0
HD2 A:LYS49 4.9 70.5 1.0
H15B B:UW8804 4.9 88.7 1.0
H9A B:UW8804 4.9 104.6 1.0
H3B B:UW8804 5.0 102.7 1.0

Reference:

J.Kreibich, J.H.Jeoung, H.Dobbek. Ligand Binding at the Ni,Ni-[4FE-4S] Cluster of Acetyl-Coa Synthase To Be Published.
Page generated: Fri Oct 11 09:15:22 2024

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