Zinc in PDB 6zeq: Aspergillus Oryzae Leucine Aminopeptidase A Mature Enzyme

The structure of Aspergillus Oryzae Leucine Aminopeptidase A Mature Enzyme, PDB code: 6zeq 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)	73.81 / 1.97
Space group	P 63 2 2
Cell size a, b, c (Å), α, β, γ (°)	153.92, 153.92, 88.64, 90, 90, 120
R / Rfree (%)	16.5 / 20.4

The structure of Aspergillus Oryzae Leucine Aminopeptidase A Mature Enzyme also contains other interesting chemical elements:

Chlorine

(Cl)

1 atom

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

Zinc binding site 1 out of 2 in the Aspergillus Oryzae Leucine Aminopeptidase A Mature Enzyme


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Aspergillus Oryzae Leucine Aminopeptidase A Mature Enzyme within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn401 b:28.8 occ:1.00 OD1 A:ASP195 2.0 28.3 1.0 O A:HOH660 2.2 34.8 1.0 NE2 A:HIS176 2.2 25.5 1.0 OD1 A:ASP261 2.2 24.6 1.0 OD2 A:ASP261 2.3 25.0 1.0 CG A:ASP261 2.6 29.2 1.0 O A:HOH699 2.7 47.3 1.0 CG A:ASP195 3.0 29.1 1.0 CD2 A:HIS176 3.2 24.9 1.0 CE1 A:HIS176 3.3 28.2 1.0 CL A:CL403 3.4 62.5 0.8 OD2 A:ASP195 3.4 24.7 1.0 ZN A:ZN402 3.6 31.9 1.0 OE1 A:GLU233 4.0 29.1 1.0 CB A:ASP196 4.0 22.5 1.0 CB A:ASP261 4.1 22.0 1.0 O A:HOH553 4.1 40.1 1.0 OE2 A:GLU234 4.2 27.6 1.0 OE2 A:GLU233 4.2 35.5 1.0 CB A:ASP195 4.2 29.2 1.0 CD A:GLU233 4.2 34.1 1.0 CG A:HIS176 4.3 28.8 1.0 ND1 A:HIS176 4.4 29.7 1.0 CA A:ASP195 4.6 27.9 1.0 CG A:ASP196 4.6 26.4 1.0 CG A:MET262 4.7 26.0 1.0 C A:ASP195 4.8 26.8 1.0 SD A:MET262 4.8 33.1 1.0 OD2 A:ASP196 4.8 29.2 1.0 CA A:ASP261 4.9 29.5 1.0 OG A:SER315 4.9 30.9 1.0 CA A:ASP196 4.9 26.2 1.0 N A:ASP196 4.9 22.6 1.0 CD A:GLU234 5.0 32.5 1.0

Zinc binding site 2 out of 2 in the Aspergillus Oryzae Leucine Aminopeptidase A Mature Enzyme


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Aspergillus Oryzae Leucine Aminopeptidase A Mature Enzyme within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn402 b:31.9 occ:0.99 OD2 A:ASP195 2.0 24.7 1.0 OE2 A:GLU234 2.0 27.6 1.0 O A:HOH660 2.2 34.8 1.0 NE2 A:HIS343 2.2 31.1 1.0 CD A:GLU234 2.7 32.5 1.0 OE1 A:GLU234 2.7 32.1 1.0 CL A:CL403 2.8 62.5 0.8 CG A:ASP195 3.0 29.1 1.0 CD2 A:HIS343 3.0 28.2 1.0 OD1 A:ASP195 3.3 28.3 1.0 CE1 A:HIS343 3.3 30.6 1.0 ZN A:ZN401 3.6 28.8 1.0 O A:HOH553 3.9 40.1 1.0 O A:HOH610 3.9 28.2 1.0 CG A:GLU234 4.2 25.4 1.0 CG A:HIS343 4.2 28.0 1.0 OE1 A:GLU233 4.2 29.1 1.0 ND1 A:HIS343 4.3 30.4 1.0 CB A:ASP195 4.3 29.2 1.0 O A:HOH699 4.4 47.3 1.0 O A:HOH670 4.4 60.6 1.0 NE2 A:HIS176 4.5 25.5 1.0 CE1 A:HIS176 4.5 28.2 1.0 O A:HOH671 4.8 48.9 1.0 CD1 A:ILE342 4.9 31.5 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