Zinc in PDB 6i5s: Ah, Bottromycin Amidohydrolase

The structure of Ah, Bottromycin Amidohydrolase, PDB code: 6i5s was solved by J.Koehnke, A.Sikandar, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	56.04 / 1.73
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	100.973, 110.726, 84.896, 90.00, 90.00, 90.00
R / Rfree (%)	15.8 / 18.9

The structure of Ah, Bottromycin Amidohydrolase also contains other interesting chemical elements:

Chlorine

(Cl)

1 atom

The binding sites of Zinc atom in the Ah, Bottromycin Amidohydrolase (pdb code 6i5s). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Ah, Bottromycin Amidohydrolase, PDB code: 6i5s:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Ah, Bottromycin Amidohydrolase


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Ah, Bottromycin Amidohydrolase within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn501 b:35.0 occ:0.61 OQ2 A:KCX183 2.0 36.1 1.0 O A:HOH605 2.1 60.4 1.0 NE2 A:HIS210 2.2 32.5 1.0 NE2 A:HIS229 2.2 28.2 1.0 O A:HOH621 2.2 39.8 1.0 O A:HOH787 2.6 43.0 1.0 CX A:KCX183 2.8 51.6 1.0 CE1 A:HIS210 2.9 39.6 1.0 CD2 A:HIS229 3.0 33.3 1.0 OQ1 A:KCX183 3.2 47.8 1.0 CE1 A:HIS229 3.2 32.3 1.0 CD2 A:HIS210 3.3 30.3 1.0 ZN A:ZN502 3.6 27.5 0.4 CE1 A:HIS94 4.0 28.9 1.0 NZ A:KCX183 4.0 39.4 1.0 OH A:TYR185 4.0 0.2 1.0 NE2 A:HIS94 4.1 34.8 1.0 ND1 A:HIS210 4.1 34.3 1.0 CG A:HIS229 4.2 29.9 1.0 ND1 A:HIS229 4.2 29.9 1.0 CE2 A:TYR185 4.3 84.9 1.0 O A:HOH620 4.3 44.4 1.0 CG A:HIS210 4.3 29.7 1.0 OD2 A:ASP348 4.4 34.3 1.0 CZ A:TYR185 4.5 0.7 1.0 CE A:KCX183 4.6 40.1 1.0 CE2 A:TYR231 4.9 32.5 1.0 OD1 A:ASP348 5.0 34.6 1.0

Zinc binding site 2 out of 2 in the Ah, Bottromycin Amidohydrolase


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Ah, Bottromycin Amidohydrolase within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn502 b:27.5 occ:0.44 OQ1 A:KCX183 2.1 47.8 1.0 NE2 A:HIS96 2.1 74.1 1.0 O A:HOH621 2.1 39.8 1.0 NE2 A:HIS94 2.1 34.8 1.0 O A:HOH620 2.2 44.4 1.0 OD1 A:ASP348 2.2 34.6 1.0 CX A:KCX183 3.0 51.6 1.0 CD2 A:HIS94 3.0 39.5 1.0 CE1 A:HIS96 3.0 80.6 1.0 CD2 A:HIS96 3.1 86.7 1.0 CG A:ASP348 3.1 33.3 1.0 CE1 A:HIS94 3.2 28.9 1.0 OQ2 A:KCX183 3.3 36.1 1.0 OD2 A:ASP348 3.4 34.3 1.0 ZN A:ZN501 3.6 35.0 0.6 O A:HOH605 4.0 60.4 1.0 NZ A:KCX183 4.1 39.4 1.0 ND1 A:HIS96 4.2 83.0 1.0 CG A:HIS94 4.2 27.8 1.0 ND1 A:HIS94 4.2 34.3 1.0 CG A:HIS96 4.2 75.6 1.0 NE2 A:HIS229 4.3 28.2 1.0 CE1 A:HIS229 4.3 32.3 1.0 CB A:ASP348 4.5 27.3 1.0 CA A:ASP348 4.8 24.5 1.0

A.Sikandar, L.Franz, O.Melse, I.Antes, J.Koehnke. Thiazoline-Specific Amidohydrolase Purah Is the Gatekeeper of Bottromycin Biosynthesis. J.Am.Chem.Soc. V. 141 9748 2019.
ISSN: ESSN 1520-5126
PubMed: 31192589
DOI: 10.1021/JACS.8B12231