Zinc in PDB 5zi5: Crystal Structure of Legionella Pneumophila Aminopeptidase A

All present enzymatic activity of Crystal Structure of Legionella Pneumophila Aminopeptidase A:
3.4.11.2;

The structure of Crystal Structure of Legionella Pneumophila Aminopeptidase A, PDB code: 5zi5 was solved by A.K.Marapaka, A.Addlagatta, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	33.05 / 2.60
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	64.543, 101.447, 129.595, 90.00, 99.29, 90.00
R / Rfree (%)	21.6 / 30.8

The binding sites of Zinc atom in the Crystal Structure of Legionella Pneumophila Aminopeptidase A (pdb code 5zi5). 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 Legionella Pneumophila Aminopeptidase A, PDB code: 5zi5:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Crystal Structure of Legionella Pneumophila Aminopeptidase A


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 Legionella Pneumophila Aminopeptidase A within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1001 b:43.3 occ:1.00 OE2 A:GLU333 2.0 35.6 1.0 O A:HOH1115 2.1 26.0 1.0 NE2 A:HIS310 2.2 39.5 1.0 NE2 A:HIS314 2.3 58.1 1.0 OE1 A:GLU333 2.7 38.8 1.0 CD A:GLU333 2.7 36.6 1.0 CD2 A:HIS314 3.0 57.3 1.0 CD2 A:HIS310 3.1 39.3 1.0 CE1 A:HIS310 3.1 41.2 1.0 CE1 A:HIS314 3.4 58.5 1.0 OH A:TYR383 3.8 49.0 1.0 CE2 A:TYR383 3.9 49.2 1.0 CZ A:TYR383 4.2 47.9 1.0 CG A:HIS314 4.2 54.0 1.0 CG A:GLU333 4.2 38.8 1.0 ND1 A:HIS310 4.3 41.4 1.0 CG A:HIS310 4.3 41.3 1.0 OE2 A:GLU311 4.3 54.4 1.0 ND1 A:HIS314 4.4 57.0 1.0 CG2 A:THR336 4.5 53.4 1.0 OE2 A:GLU277 4.7 44.8 1.0 CA A:GLU333 4.7 40.4 1.0 CB A:THR336 4.8 54.2 1.0 OE1 A:GLU277 4.8 43.4 1.0 CB A:GLU333 4.8 39.0 1.0 CD2 A:TYR383 4.8 47.8 1.0 CD A:GLU277 4.9 44.8 1.0 CD A:GLU311 5.0 54.3 1.0

Zinc binding site 2 out of 2 in the Crystal Structure of Legionella Pneumophila Aminopeptidase A


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 Legionella Pneumophila Aminopeptidase A within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn1001 b:46.3 occ:1.00 NE2 B:HIS314 2.2 47.9 1.0 O B:HOH1110 2.2 42.2 1.0 OE2 B:GLU333 2.2 38.4 1.0 NE2 B:HIS310 2.3 45.9 1.0 OE1 B:GLU333 2.8 38.5 1.0 CD2 B:HIS314 2.8 48.9 1.0 CD B:GLU333 2.8 41.0 1.0 CD2 B:HIS310 3.2 48.1 1.0 CE1 B:HIS314 3.3 50.2 1.0 CE1 B:HIS310 3.4 48.8 1.0 CG B:HIS314 4.0 45.6 1.0 CE2 B:TYR383 4.0 51.2 1.0 OH B:TYR383 4.2 51.3 1.0 ND1 B:HIS314 4.3 50.6 1.0 CG B:GLU333 4.3 39.9 1.0 CG B:HIS310 4.4 46.6 1.0 OE1 B:GLU277 4.4 54.2 1.0 ND1 B:HIS310 4.4 49.5 1.0 OE2 B:GLU311 4.5 50.9 1.0 CZ B:TYR383 4.5 51.3 1.0 OE1 B:GLU311 4.6 52.6 1.0 CA B:GLU333 4.8 39.4 1.0 CG2 B:THR336 4.8 45.6 1.0 CB B:GLU333 4.9 38.5 1.0 CD B:GLU311 4.9 47.9 1.0 NZ B:LYS332 4.9 44.8 1.0 CD2 B:TYR383 4.9 51.0 1.0 CB B:THR336 4.9 48.1 1.0

A.K.Marapaka, V.Pillalamarri, R.Gumpena, N.Haque, S.C.Bala, A.Jangam, A.Addlagatta. Discovery, Structural and Biochemical Studies of A Rare Glu/Asp Specific M1 Class Aminopeptidase From Legionella Pneumophila Int. J. Biol. Macromol. V. 120 1111 2018.
ISSN: ISSN 1879-0003
PubMed: 30172821
DOI: 10.1016/J.IJBIOMAC.2018.08.172