Zinc in PDB 6zep: Flavourzyme Leucine Aminopeptidase A Proenzyme

The structure of Flavourzyme Leucine Aminopeptidase A Proenzyme, PDB code: 6zep was solved by K.A.Watson, G.Baltulionis, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	42.61 / 1.61
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	43.43, 94.39, 99.11, 90, 90, 90
R / Rfree (%)	15.3 / 17.4

The structure of Flavourzyme Leucine Aminopeptidase A Proenzyme also contains other interesting chemical elements:

Chlorine

(Cl)

1 atom

The binding sites of Zinc atom in the Flavourzyme Leucine Aminopeptidase A Proenzyme (pdb code 6zep). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Flavourzyme Leucine Aminopeptidase A Proenzyme, PDB code: 6zep:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Flavourzyme Leucine Aminopeptidase A Proenzyme


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Flavourzyme Leucine Aminopeptidase A Proenzyme within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn409 b:16.9 occ:1.00 OD1 A:ASP195 2.0 17.3 1.0 O A:HOH693 2.1 20.1 1.0 NE2 A:HIS176 2.1 13.8 1.0 OD1 A:ASP261 2.2 16.6 1.0 OD2 A:ASP261 2.3 19.7 1.0 O A:HOH800 2.4 24.3 1.0 CG A:ASP261 2.6 19.1 1.0 CG A:ASP195 3.0 16.2 1.0 CE1 A:HIS176 3.1 14.8 1.0 CD2 A:HIS176 3.1 12.9 1.0 ZN A:ZN410 3.4 20.9 1.0 OD2 A:ASP195 3.5 17.7 1.0 CL A:CL411 3.5 50.5 1.0 O A:HOH735 3.9 39.3 1.0 OE1 A:GLU233 3.9 19.9 1.0 OE1 A:GLU234 4.1 20.0 1.0 CB A:ASP261 4.1 15.6 1.0 CB A:ASP196 4.2 14.0 1.0 O A:HOH730 4.2 32.1 1.0 ND1 A:HIS176 4.2 14.2 1.0 OE2 A:GLU233 4.2 25.5 1.0 CB A:ASP195 4.3 15.2 1.0 CG A:HIS176 4.3 12.5 1.0 CD A:GLU233 4.3 20.7 1.0 CA A:ASP195 4.6 14.2 1.0 O A:HOH829 4.7 43.0 1.0 C A:ASP195 4.7 16.2 1.0 CG A:MET262 4.7 18.2 1.0 CG A:ASP196 4.8 13.9 1.0 N A:ASP196 4.8 14.7 1.0 CD A:GLU234 4.8 23.0 1.0 CA A:ASP261 4.9 14.4 1.0 SD A:MET262 4.9 20.1 1.0 CA A:ASP196 4.9 14.6 1.0

Zinc binding site 2 out of 2 in the Flavourzyme Leucine Aminopeptidase A Proenzyme


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Flavourzyme Leucine Aminopeptidase A Proenzyme within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn410 b:20.9 occ:1.00 OD2 A:ASP195 2.0 17.7 1.0 NE2 A:HIS343 2.0 22.8 1.0 OE1 A:GLU234 2.1 20.0 1.0 O A:HOH693 2.2 20.1 1.0 CL A:CL411 2.4 50.5 1.0 CD A:GLU234 2.8 23.0 1.0 OE2 A:GLU234 2.9 21.1 1.0 CG A:ASP195 2.9 16.2 1.0 CD2 A:HIS343 2.9 17.6 1.0 CE1 A:HIS343 3.1 25.9 1.0 OD1 A:ASP195 3.2 17.3 1.0 ZN A:ZN409 3.4 16.9 1.0 O A:HOH800 3.5 24.3 1.0 NH2 A:ARG50 3.8 42.9 1.0 O A:HOH735 3.9 39.3 1.0 NH2 A:ARG55 4.0 43.0 0.6 O A:HOH610 4.1 18.5 1.0 CG A:HIS343 4.1 22.6 1.0 ND1 A:HIS343 4.1 24.4 1.0 CG A:GLU234 4.3 17.9 1.0 CB A:ASP195 4.3 15.2 1.0 OE1 A:GLU233 4.4 19.9 1.0 NE2 A:HIS176 4.6 13.8 1.0 CE1 A:HIS176 4.7 14.8 1.0 CD1 A:ILE342 4.8 22.8 1.0 O A:HOH829 4.9 43.0 1.0 O A:HOH745 4.9 55.3 1.0 CZ A:ARG50 5.0 41.0 1.0

G.Baltulionis, M.Blight, A.Robin, D.Charalampopoulos, K.A.Watson. The Role of Propeptide-Mediated Autoinhibition and Intermolecular Chaperone in the Maturation of Cognate Catalytic Domain in Leucine Aminopeptidase. J.Struct.Biol. V. 213 07741 2021.
ISSN: ESSN 1095-8657
PubMed: 33989771
DOI: 10.1016/J.JSB.2021.107741