Zinc in PDB 6os6: Crystal Structure of Cymd Prenyltransferase Complexed with L- Tryptophan and Dmspp

The structure of Crystal Structure of Cymd Prenyltransferase Complexed with L- Tryptophan and Dmspp, PDB code: 6os6 was solved by B.W.Roose, D.W.Christianson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	29.12 / 1.33
Space group	I 4
Cell size a, b, c (Å), α, β, γ (°)	129.446, 129.446, 49.777, 90.00, 90.00, 90.00
R / Rfree (%)	16.6 / 18.1

The structure of Crystal Structure of Cymd Prenyltransferase Complexed with L- Tryptophan and Dmspp also contains other interesting chemical elements:

Chlorine

(Cl)

1 atom

The binding sites of Zinc atom in the Crystal Structure of Cymd Prenyltransferase Complexed with L- Tryptophan and Dmspp (pdb code 6os6). 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 Cymd Prenyltransferase Complexed with L- Tryptophan and Dmspp, PDB code: 6os6:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Crystal Structure of Cymd Prenyltransferase Complexed with L- Tryptophan and Dmspp


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 Cymd Prenyltransferase Complexed with L- Tryptophan and Dmspp within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn403 b:14.9 occ:1.00 OE1 A:GLU3 1.9 22.4 1.0 CL A:CL405 2.3 16.4 1.0 CD A:GLU3 2.6 22.5 1.0 OE2 A:GLU3 2.7 26.7 1.0 CG A:GLU3 4.0 20.6 1.0 O A:HOH707 4.6 36.3 1.0 CB A:GLU3 4.9 21.8 1.0

Zinc binding site 2 out of 2 in the Crystal Structure of Cymd Prenyltransferase Complexed with L- Tryptophan and Dmspp


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 Cymd Prenyltransferase Complexed with L- Tryptophan and Dmspp within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn404 b:12.9 occ:1.00 OD1 A:ASP50 2.0 12.3 1.0 NE2 A:HIS49 2.1 13.2 1.0 O2 A:BEZ406 2.1 19.4 1.0 O1 A:BEZ406 2.3 15.8 1.0 C A:BEZ406 2.6 14.3 1.0 CG A:ASP50 2.7 13.6 1.0 OD2 A:ASP50 2.7 13.6 1.0 CE1 A:HIS49 3.0 14.2 1.0 CD2 A:HIS49 3.0 12.8 1.0 C1 A:BEZ406 4.1 16.5 1.0 ND1 A:HIS49 4.1 13.6 1.0 CG A:HIS49 4.1 12.8 1.0 CB A:ASP50 4.1 12.5 1.0 O A:HOH571 4.2 28.7 1.0 H6 A:BEZ406 4.7 22.4 1.0 CA A:ASP50 4.7 10.7 1.0 H2 A:BEZ406 4.8 19.8 1.0 C6 A:BEZ406 4.9 18.7 1.0 N A:ASP50 4.9 11.0 1.0 C2 A:BEZ406 4.9 16.5 1.0

B.W.Roose, D.W.Christianson. Structural Basis of Tryptophan Reverse N-Prenylation Catalyzed By Cymd. Biochemistry V. 58 3232 2019.
ISSN: ISSN 0006-2960
PubMed: 31251043
DOI: 10.1021/ACS.BIOCHEM.9B00399