Zinc in PDB 6esl: Crystal Structure of the Legionella Pneumoppila Lapa

All present enzymatic activity of Crystal Structure of the Legionella Pneumoppila Lapa:
3.4.11.10;

The structure of Crystal Structure of the Legionella Pneumoppila Lapa, PDB code: 6esl was solved by K.Richardson, J.A.Garnett, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	99.56 / 1.87
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	76.597, 99.556, 104.012, 90.00, 90.00, 90.00
R / Rfree (%)	19.2 / 23.8

The binding sites of Zinc atom in the Crystal Structure of the Legionella Pneumoppila Lapa (pdb code 6esl). 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 the Legionella Pneumoppila Lapa, PDB code: 6esl:
Jump to Zinc binding site number: 1; 2; 3; 4;

Zinc binding site 1 out of 4 in the Crystal Structure of the Legionella Pneumoppila Lapa


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 the Legionella Pneumoppila Lapa within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn401 b:75.8 occ:1.00 OD2 A:ASP207 1.9 29.2 1.0 OE2 A:GLU242 2.3 31.6 1.0 NE2 A:HIS347 2.7 35.2 1.0 OE1 A:GLU242 2.9 28.9 1.0 CD A:GLU242 2.9 29.8 1.0 CG A:ASP207 3.0 26.9 1.0 ZN A:ZN402 3.2 26.5 1.0 O A:HOH629 3.2 22.5 1.0 OD1 A:ASP207 3.5 22.9 1.0 CE1 A:HIS347 3.5 33.0 1.0 CD2 A:HIS347 3.7 33.2 1.0 OE1 A:GLU241 4.1 26.3 1.0 CB A:ASP207 4.2 25.5 1.0 CE1 A:HIS194 4.4 25.4 1.0 NE2 A:HIS194 4.4 23.7 1.0 CG A:GLU242 4.4 28.0 1.0 O A:HOH535 4.5 33.2 1.0 ND1 A:HIS347 4.6 31.6 1.0 CG A:HIS347 4.8 31.5 1.0 CD A:GLU241 4.9 27.0 1.0 OD2 A:ASP269 5.0 22.3 1.0

Zinc binding site 2 out of 4 in the Crystal Structure of the Legionella Pneumoppila Lapa


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 the Legionella Pneumoppila Lapa within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn402 b:26.5 occ:1.00 OD1 A:ASP207 1.9 22.9 1.0 NE2 A:HIS194 2.1 23.7 1.0 OD2 A:ASP269 2.2 22.3 1.0 O A:HOH629 2.2 22.5 1.0 OD1 A:ASP269 2.3 24.5 1.0 CG A:ASP269 2.5 23.2 1.0 CG A:ASP207 2.6 26.9 1.0 OD2 A:ASP207 2.9 29.2 1.0 CE1 A:HIS194 3.0 25.4 1.0 CD2 A:HIS194 3.2 24.2 1.0 ZN A:ZN401 3.2 75.8 1.0 CB A:ASP207 3.9 25.5 1.0 CB A:ASP269 4.0 21.9 1.0 OE1 A:GLU241 4.1 26.3 1.0 CB A:ASP208 4.1 24.8 1.0 OE2 A:GLU242 4.2 31.6 1.0 ND1 A:HIS194 4.2 24.0 1.0 CG A:HIS194 4.3 24.3 1.0 CD A:GLU241 4.4 27.0 1.0 CA A:ASP207 4.5 24.7 1.0 CG A:MET270 4.6 27.3 1.0 OE2 A:GLU241 4.7 30.3 1.0 OG A:SER319 4.7 24.2 1.0 CG A:ASP208 4.7 25.2 1.0 C A:ASP207 4.8 23.8 1.0 CA A:ASP269 4.8 23.3 1.0 N A:ASP208 4.9 24.4 1.0 SD A:MET270 4.9 28.9 1.0 CA A:ASP208 4.9 24.8 1.0 CD A:GLU242 5.0 29.8 1.0 OD2 A:ASP208 5.0 24.3 1.0

Zinc binding site 3 out of 4 in the Crystal Structure of the Legionella Pneumoppila Lapa


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 the Legionella Pneumoppila Lapa within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn401 b:74.3 occ:1.00 OD2 B:ASP207 2.5 26.3 1.0 OE2 B:GLU242 2.6 28.6 1.0 ZN B:ZN402 2.7 23.9 1.0 O B:HOH511 2.9 17.3 1.0 OD1 B:ASP207 3.0 22.7 1.0 CD B:GLU242 3.1 25.5 1.0 OE1 B:GLU242 3.1 26.0 1.0 CG B:ASP207 3.1 25.0 1.0 NE2 B:HIS347 3.2 31.0 1.0 OE1 B:GLU241 3.5 24.8 1.0 NE2 B:HIS194 3.9 22.0 1.0 CE1 B:HIS194 4.0 22.0 1.0 CE1 B:HIS347 4.0 28.2 1.0 O B:HOH510 4.2 37.0 1.0 CD2 B:HIS347 4.2 29.6 1.0 CD B:GLU241 4.3 23.9 1.0 CG B:GLU242 4.4 24.6 1.0 OD2 B:ASP269 4.5 21.5 1.0 OE2 B:GLU241 4.5 27.9 1.0 CB B:ASP207 4.6 22.3 1.0 O B:HOH548 4.6 30.8 1.0 OD1 B:ASP269 4.8 23.7 1.0

Zinc binding site 4 out of 4 in the Crystal Structure of the Legionella Pneumoppila Lapa


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 the Legionella Pneumoppila Lapa within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn402 b:23.9 occ:1.00 OD1 B:ASP207 2.0 22.7 1.0 NE2 B:HIS194 2.2 22.0 1.0 O B:HOH511 2.2 17.3 1.0 OD1 B:ASP269 2.4 23.7 1.0 OD2 B:ASP269 2.5 21.5 1.0 ZN B:ZN401 2.7 74.3 1.0 CG B:ASP269 2.7 22.6 1.0 CG B:ASP207 3.0 25.0 1.0 CE1 B:HIS194 3.1 22.0 1.0 CD2 B:HIS194 3.2 22.6 1.0 OD2 B:ASP207 3.4 26.3 1.0 OE1 B:GLU241 4.0 24.8 1.0 CB B:ASP269 4.1 20.9 1.0 CB B:ASP208 4.2 19.9 1.0 ND1 B:HIS194 4.2 23.1 1.0 OE2 B:GLU242 4.2 28.6 1.0 CB B:ASP207 4.3 22.3 1.0 CG B:HIS194 4.3 22.5 1.0 CD B:GLU241 4.3 23.9 1.0 CG B:MET270 4.6 21.2 1.0 OE2 B:GLU241 4.6 27.9 1.0 CA B:ASP207 4.6 23.0 1.0 OG B:SER319 4.7 20.4 1.0 CG B:ASP208 4.8 19.7 1.0 CA B:ASP269 4.8 21.0 1.0 SD B:MET270 4.9 24.2 1.0 C B:ASP207 4.9 21.2 1.0 N B:ASP208 4.9 20.6 1.0 CA B:ASP208 5.0 20.6 1.0 CD B:GLU242 5.0 25.5 1.0

R.C.White, F.F.Gunderson, J.Y.Tyson, K.H.Richardson, T.J.Portlock, J.A.Garnett, N.P.Cianciotto. Type II Secretion-Dependent Aminopeptidase Lapa and Acyltransferase Plac Are Redundant For Nutrient Acquisition Duringlegionella Pneumophilaintracellular Infection of Amoebas. Mbio V. 9 2018.
ISSN: ESSN 2150-7511
PubMed: 29666285
DOI: 10.1128/MBIO.00528-18