Zinc in PDB 8avz: Crystal Structure of Pksd, the Trans-Acting Acyl Hydrolase Domain From the Bacillaene Trans-at Pks (Semet Derivative)

The structure of Crystal Structure of Pksd, the Trans-Acting Acyl Hydrolase Domain From the Bacillaene Trans-at Pks (Semet Derivative), PDB code: 8avz was solved by C.D.Fage, G.L.Challis, J.Lewandowski, M.Jenner, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	59.79 / 1.96
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	207.708, 83.564, 145.742, 90, 119.71, 90
R / Rfree (%)	17.9 / 20.3

The binding sites of Zinc atom in the Crystal Structure of Pksd, the Trans-Acting Acyl Hydrolase Domain From the Bacillaene Trans-at Pks (Semet Derivative) (pdb code 8avz). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Crystal Structure of Pksd, the Trans-Acting Acyl Hydrolase Domain From the Bacillaene Trans-at Pks (Semet Derivative), PDB code: 8avz:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Crystal Structure of Pksd, the Trans-Acting Acyl Hydrolase Domain From the Bacillaene Trans-at Pks (Semet Derivative)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of Pksd, the Trans-Acting Acyl Hydrolase Domain From the Bacillaene Trans-at Pks (Semet Derivative) within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn401 b:44.1 occ:1.00 NE2 A:HIS238 2.0 43.5 1.0 NE2 C:HIS238 2.0 36.2 1.0 SG C:CYS236 2.3 44.7 1.0 SG A:CYS236 2.4 44.5 1.0 CD2 A:HIS238 2.9 43.2 1.0 CD2 C:HIS238 3.0 37.4 1.0 CE1 A:HIS238 3.0 39.4 1.0 CE1 C:HIS238 3.0 36.0 1.0 CB C:CYS236 3.0 35.9 1.0 CB A:CYS236 3.2 41.0 1.0 OH C:TYR261 3.7 55.1 1.0 ND1 A:HIS238 4.1 45.4 1.0 CG A:HIS238 4.1 42.7 1.0 ND1 C:HIS238 4.1 38.2 1.0 CG C:HIS238 4.1 37.5 1.0 O A:HOH561 4.2 42.5 1.0 CA C:CYS236 4.4 36.1 1.0 O A:HOH664 4.5 48.0 1.0 CA A:CYS236 4.5 43.3 1.0 CZ C:TYR261 4.5 52.2 1.0 C A:CYS236 4.7 47.0 1.0 C C:CYS236 4.9 37.4 1.0 CE2 C:TYR261 4.9 50.9 1.0 CB A:PRO227 5.0 36.5 1.0

Zinc binding site 2 out of 2 in the Crystal Structure of Pksd, the Trans-Acting Acyl Hydrolase Domain From the Bacillaene Trans-at Pks (Semet Derivative)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Crystal Structure of Pksd, the Trans-Acting Acyl Hydrolase Domain From the Bacillaene Trans-at Pks (Semet Derivative) within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn401 b:46.0 occ:1.00 NE2 B:HIS238 1.9 36.4 1.0 NE2 D:HIS238 2.0 37.6 1.0 SG D:CYS236 2.3 46.8 1.0 SG B:CYS236 2.3 44.4 1.0 CE1 B:HIS238 2.9 42.9 1.0 CD2 B:HIS238 2.9 44.1 1.0 CD2 D:HIS238 2.9 35.8 1.0 CE1 D:HIS238 3.1 35.7 1.0 CB D:CYS236 3.1 38.9 1.0 CB B:CYS236 3.2 40.6 1.0 OH D:TYR261 3.8 51.3 1.0 ND1 B:HIS238 4.0 46.3 1.0 CG B:HIS238 4.0 40.9 1.0 CG D:HIS238 4.1 33.9 1.0 ND1 D:HIS238 4.1 41.9 1.0 O B:HOH547 4.3 41.9 1.0 O D:HOH467 4.4 49.3 1.0 CA B:CYS236 4.5 40.5 1.0 CA D:CYS236 4.5 38.8 1.0 CZ D:TYR261 4.6 48.9 1.0 C B:CYS236 4.7 44.9 1.0 OH B:TYR261 4.7 64.4 1.0 O B:HOH667 4.7 47.5 1.0 CE2 D:TYR261 4.9 45.6 1.0 C D:CYS236 4.9 35.9 1.0 O B:CYS236 4.9 48.5 1.0 CB B:PRO227 5.0 38.5 1.0

C.D.Fage, M.Passmore, B.Tatman, H.G.Smith, X.Jian, U.C.M.Mudiyanselage, M.Berger, A.G.Cisneros, G.L.Challis, J.R.Lewandowski, M.Jenner. Structural Basis For Acyl Hydrolysis in Trans-at Polyketide Synthases To Be Published.