Zinc in PDB 5m3k: A Multi-Component Acyltransferase Phlabc From Pseudomonas Protegens

The structure of A Multi-Component Acyltransferase Phlabc From Pseudomonas Protegens, PDB code: 5m3k was solved by T.Pavkov-Keller, N.G.Schmidt, W.Kroutil, K.Gruber, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	49.86 / 2.83
Space group	P 61 2 2
Cell size a, b, c (Å), α, β, γ (°)	222.626, 222.626, 237.099, 90.00, 90.00, 120.00
R / Rfree (%)	16.7 / 19.6

The binding sites of Zinc atom in the A Multi-Component Acyltransferase Phlabc From Pseudomonas Protegens (pdb code 5m3k). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the A Multi-Component Acyltransferase Phlabc From Pseudomonas Protegens, PDB code: 5m3k:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the A Multi-Component Acyltransferase Phlabc From Pseudomonas Protegens


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of A Multi-Component Acyltransferase Phlabc From Pseudomonas Protegens within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn200 b:35.8 occ:1.00 SG B:CYS34 2.3 34.5 1.0 SG B:CYS48 2.3 31.7 1.0 SG B:CYS37 2.3 34.6 1.0 SG B:CYS51 2.3 35.7 1.0 CB B:CYS34 3.2 34.8 1.0 CB B:CYS48 3.3 33.4 1.0 CB B:CYS37 3.4 37.0 1.0 CB B:CYS51 3.4 36.8 1.0 N B:CYS37 3.9 40.7 1.0 N B:CYS51 3.9 36.4 1.0 CA B:CYS37 4.2 38.6 1.0 CA B:CYS51 4.2 37.1 1.0 CB B:ALA50 4.5 35.0 1.0 CA B:CYS34 4.7 35.4 1.0 CB B:SER53 4.7 40.8 1.0 CA B:CYS48 4.7 33.2 1.0 C B:CYS51 4.8 37.6 1.0 CB B:GLU36 4.8 48.2 1.0 C B:CYS37 4.9 38.0 1.0 C B:ALA50 4.9 36.4 1.0 C B:GLU36 5.0 44.0 1.0 N B:ASN52 5.0 37.1 1.0

Zinc binding site 2 out of 2 in the A Multi-Component Acyltransferase Phlabc From Pseudomonas Protegens


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of A Multi-Component Acyltransferase Phlabc From Pseudomonas Protegens within 5.0Å range: probe atom residue distance (Å) B Occ E:Zn200 b:31.7 occ:1.00 SG E:CYS51 2.3 31.7 1.0 SG E:CYS37 2.3 30.7 1.0 SG E:CYS34 2.3 31.8 1.0 SG E:CYS48 2.3 28.9 1.0 CB E:CYS34 3.2 31.9 1.0 CB E:CYS48 3.3 30.2 1.0 CB E:CYS51 3.4 32.4 1.0 CB E:CYS37 3.4 33.3 1.0 N E:CYS51 3.9 32.2 1.0 N E:CYS37 3.9 37.1 1.0 CA E:CYS51 4.2 32.9 1.0 CA E:CYS37 4.2 34.5 1.0 CB E:ALA50 4.5 31.8 1.0 CB E:SER53 4.7 32.8 1.0 CA E:CYS34 4.7 33.2 1.0 CA E:CYS48 4.8 30.4 1.0 C E:CYS51 4.8 33.4 1.0 CB E:GLU36 4.8 45.0 1.0 C E:ALA50 4.9 32.1 1.0 C E:CYS37 4.9 33.7 1.0 C E:GLU36 5.0 40.2 1.0

T.Pavkov-Keller, N.G.Schmidt, A.Zadlo-Dobrowolska, W.Kroutil, K.Gruber. Structure and Catalytic Mechanism of A Bacterial Friedel-Crafts Acylase. Chembiochem V. 20 88 2019.
ISSN: ESSN 1439-7633
PubMed: 30318713
DOI: 10.1002/CBIC.201800462