Zinc in PDB 8aw0: Crystal Structure of Pksd, the Trans-Acting Acyl Hydrolase Domain From the Bacillaene Trans-at Pks (Native)

The structure of Crystal Structure of Pksd, the Trans-Acting Acyl Hydrolase Domain From the Bacillaene Trans-at Pks (Native), PDB code: 8aw0 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)	51.08 / 2.20
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	151.202, 163.33, 186.871, 90, 104.5, 90
R / Rfree (%)	19.8 / 22.7

The binding sites of Zinc atom in the Crystal Structure of Pksd, the Trans-Acting Acyl Hydrolase Domain From the Bacillaene Trans-at Pks (Native) (pdb code 8aw0). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the Crystal Structure of Pksd, the Trans-Acting Acyl Hydrolase Domain From the Bacillaene Trans-at Pks (Native), PDB code: 8aw0:
Jump to Zinc binding site number: 1; 2; 3; 4;

Zinc binding site 1 out of 4 in the Crystal Structure of Pksd, the Trans-Acting Acyl Hydrolase Domain From the Bacillaene Trans-at Pks (Native)


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 (Native) within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn401 b:80.7 occ:1.00 NE2 F:HIS238 2.0 74.9 1.0 NE2 A:HIS238 2.0 70.3 1.0 CE1 A:HIS238 2.3 71.5 1.0 SG A:CYS236 2.3 94.4 1.0 SG F:CYS236 2.3 102.7 1.0 CE1 F:HIS238 2.9 74.2 1.0 CD2 F:HIS238 3.0 69.2 1.0 CB F:CYS236 3.2 73.6 1.0 CB A:CYS236 3.3 73.8 1.0 CD2 A:HIS238 3.4 74.3 1.0 ND1 A:HIS238 3.6 87.0 1.0 OH A:TYR261 4.0 104.9 1.0 ND1 F:HIS238 4.1 71.7 1.0 CG A:HIS238 4.1 76.1 1.0 CG F:HIS238 4.1 70.5 1.0 OH F:TYR261 4.3 102.0 1.0 CA F:CYS236 4.5 76.0 1.0 CA A:CYS236 4.7 74.8 1.0 C F:CYS236 4.8 71.2 1.0 C A:CYS236 4.9 77.8 1.0 N F:LEU237 4.9 69.8 1.0

Zinc binding site 2 out of 4 in the Crystal Structure of Pksd, the Trans-Acting Acyl Hydrolase Domain From the Bacillaene Trans-at Pks (Native)


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 (Native) within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn401 b:68.8 occ:1.00 NE2 B:HIS238 2.0 65.2 1.0 NE2 D:HIS238 2.0 69.8 1.0 SG B:CYS236 2.3 76.9 1.0 SG D:CYS236 2.3 78.2 1.0 CD2 B:HIS238 2.9 66.0 1.0 CD2 D:HIS238 3.0 60.3 1.0 CE1 D:HIS238 3.1 61.6 1.0 CE1 B:HIS238 3.1 70.0 1.0 CB B:CYS236 3.2 73.8 1.0 CB D:CYS236 3.3 68.6 1.0 OH D:TYR261 3.8 81.4 1.0 CG B:HIS238 4.1 72.2 1.0 ND1 B:HIS238 4.1 74.9 1.0 CG D:HIS238 4.1 66.5 1.0 O B:HOH519 4.1 76.9 1.0 ND1 D:HIS238 4.2 69.2 1.0 OH B:TYR261 4.2 90.5 1.0 CA B:CYS236 4.6 70.5 1.0 CZ D:TYR261 4.7 66.5 1.0 CA D:CYS236 4.7 61.0 1.0 C B:CYS236 4.8 73.7 1.0 CB B:PRO227 4.9 66.5 1.0

Zinc binding site 3 out of 4 in the Crystal Structure of Pksd, the Trans-Acting Acyl Hydrolase Domain From the Bacillaene Trans-at Pks (Native)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Crystal Structure of Pksd, the Trans-Acting Acyl Hydrolase Domain From the Bacillaene Trans-at Pks (Native) within 5.0Å range: probe atom residue distance (Å) B Occ C:Zn401 b:76.5 occ:1.00 NE2 C:HIS238 2.0 63.9 1.0 NE2 H:HIS238 2.0 72.2 1.0 SG C:CYS236 2.3 78.7 1.0 SG H:CYS236 2.3 77.9 1.0 CE1 C:HIS238 3.0 72.1 1.0 CE1 H:HIS238 3.0 66.9 1.0 CD2 C:HIS238 3.0 77.5 1.0 CD2 H:HIS238 3.0 66.7 1.0 CB C:CYS236 3.2 71.8 1.0 CB H:CYS236 3.3 72.4 1.0 OH H:TYR261 3.8 84.6 1.0 ND1 C:HIS238 4.1 78.0 1.0 ND1 H:HIS238 4.1 64.7 1.0 CG C:HIS238 4.1 77.5 1.0 CG H:HIS238 4.1 67.6 1.0 OH C:TYR261 4.3 99.8 1.0 CA C:CYS236 4.6 67.8 1.0 CZ H:TYR261 4.7 85.2 1.0 CA H:CYS236 4.7 75.1 1.0 C C:CYS236 4.8 74.7 1.0 CB C:PRO227 4.8 66.3 1.0

Zinc binding site 4 out of 4 in the Crystal Structure of Pksd, the Trans-Acting Acyl Hydrolase Domain From the Bacillaene Trans-at Pks (Native)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Crystal Structure of Pksd, the Trans-Acting Acyl Hydrolase Domain From the Bacillaene Trans-at Pks (Native) within 5.0Å range: probe atom residue distance (Å) B Occ E:Zn401 b:76.4 occ:1.00 NE2 E:HIS238 2.0 74.7 1.0 SG E:CYS236 2.3 76.0 1.0 CD2 E:HIS238 3.0 77.0 1.0 CE1 E:HIS238 3.0 75.9 1.0 CB E:CYS236 3.2 76.5 1.0 OH E:TYR261 3.9 78.0 1.0 ND1 E:HIS238 4.1 72.5 1.0 CG E:HIS238 4.1 75.5 1.0 CA E:CYS236 4.5 75.3 1.0 C E:CYS236 4.8 76.9 1.0 CB E:PRO227 4.8 69.0 1.0 CZ E:TYR261 5.0 86.7 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.