Zinc in PDB 4lx9: Archaeal Amino-Terminal Acetyltransferase (Nat) Bound to Acetyl Coenzyme A

The structure of Archaeal Amino-Terminal Acetyltransferase (Nat) Bound to Acetyl Coenzyme A, PDB code: 4lx9 was solved by G.P.Liszczak, R.Marmorstein, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	21.05 / 1.98
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	100.840, 35.062, 51.219, 90.00, 100.05, 90.00
R / Rfree (%)	19.9 / 24.2

The binding sites of Zinc atom in the Archaeal Amino-Terminal Acetyltransferase (Nat) Bound to Acetyl Coenzyme A (pdb code 4lx9). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Archaeal Amino-Terminal Acetyltransferase (Nat) Bound to Acetyl Coenzyme A, PDB code: 4lx9:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Archaeal Amino-Terminal Acetyltransferase (Nat) Bound to Acetyl Coenzyme A


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Archaeal Amino-Terminal Acetyltransferase (Nat) Bound to Acetyl Coenzyme A within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn302 b:17.8 occ:1.00 OE1 A:GLU176 1.9 14.5 1.0 NE2 A:HIS137 2.1 12.1 1.0 O A:HOH520 2.2 14.3 1.0 O A:HOH412 2.3 18.3 1.0 O A:HOH405 2.3 10.1 1.0 CD A:GLU176 2.7 13.4 1.0 OE2 A:GLU176 2.8 14.3 1.0 CE1 A:HIS137 3.0 13.0 1.0 CD2 A:HIS137 3.2 10.8 1.0 O A:HOH456 3.9 13.7 1.0 O A:VAL138 4.1 11.8 1.0 CG A:GLU176 4.1 15.2 1.0 N A:GLU176 4.1 13.3 1.0 ND1 A:HIS137 4.2 13.1 1.0 CG A:HIS137 4.3 9.9 1.0 OH A:TYR202 4.4 20.4 1.0 O A:HOH454 4.4 29.9 1.0 CA A:VAL139 4.4 10.5 1.0 O A:VAL139 4.5 13.2 1.0 O A:HOH485 4.6 40.0 1.0 CB A:GLU176 4.6 13.4 1.0 CA A:LEU175 4.7 9.8 1.0 C A:LEU175 4.8 11.8 1.0 C A:VAL138 4.9 13.2 1.0 C A:VAL139 4.9 13.4 1.0 CA A:GLU176 5.0 12.3 1.0

Zinc binding site 2 out of 2 in the Archaeal Amino-Terminal Acetyltransferase (Nat) Bound to Acetyl Coenzyme A


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Archaeal Amino-Terminal Acetyltransferase (Nat) Bound to Acetyl Coenzyme A within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn303 b:50.0 occ:1.00 OD1 A:ASP167 2.1 28.5 1.0 OD2 A:ASP167 2.7 19.8 1.0 CG A:ASP167 2.7 20.4 1.0 O A:HOH438 3.8 27.6 1.0 CB A:ASP167 4.2 16.7 1.0 O A:HOH434 4.4 30.5 1.0 CD1 A:LEU100 4.7 24.9 1.0 CA A:ASP167 4.9 18.0 1.0 CD2 A:LEU100 5.0 24.4 1.0

G.Liszczak, R.Marmorstein. Implications For the Evolution of Eukaryotic Amino-Terminal Acetyltransferase (Nat) Enzymes From the Structure of An Archaeal Ortholog. Proc.Natl.Acad.Sci.Usa V. 110 14652 2013.
ISSN: ISSN 0027-8424
PubMed: 23959863
DOI: 10.1073/PNAS.1310365110