Zinc in PDB 2o53: Crystal Structure of Apo-Aspartoacylase From Human Brain

All present enzymatic activity of Crystal Structure of Apo-Aspartoacylase From Human Brain:
3.5.1.15;

The structure of Crystal Structure of Apo-Aspartoacylase From Human Brain, PDB code: 2o53 was solved by J.Le Coq, A.Pavlovsky, R.Sanishvili, R.E.Viola, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.00 / 2.70
Space group	P 42 21 2
Cell size a, b, c (Å), α, β, γ (°)	143.794, 143.794, 104.076, 90.00, 90.00, 90.00
R / Rfree (%)	21.6 / 26.9

The binding sites of Zinc atom in the Crystal Structure of Apo-Aspartoacylase From Human Brain (pdb code 2o53). 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 Apo-Aspartoacylase From Human Brain, PDB code: 2o53:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Crystal Structure of Apo-Aspartoacylase From Human Brain


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 Apo-Aspartoacylase From Human Brain within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn314 b:59.3 occ:1.00 ND1 A:HIS21 2.1 40.2 1.0 O4 A:PO4315 2.3 52.9 0.5 OE1 A:GLU24 2.3 45.1 1.0 ND1 A:HIS116 2.4 40.6 1.0 O3 A:PO4315 2.7 53.1 0.5 OE2 A:GLU24 2.7 44.5 1.0 P A:PO4315 2.7 53.9 0.5 CD A:GLU24 2.8 43.9 1.0 CE1 A:HIS21 2.8 40.5 1.0 O2 A:PO4315 3.0 53.0 0.5 CG A:HIS116 3.2 38.5 1.0 CE1 A:HIS116 3.3 38.9 1.0 CG A:HIS21 3.3 40.9 1.0 CB A:HIS116 3.5 37.6 1.0 CB A:HIS21 3.9 40.6 1.0 NE2 A:HIS21 4.0 39.9 1.0 O1 A:PO4315 4.2 53.8 0.5 CG A:GLU24 4.2 42.2 1.0 CA A:HIS116 4.2 37.5 1.0 CD2 A:HIS21 4.3 39.7 1.0 O A:ASN117 4.3 38.9 1.0 NH1 A:ARG63 4.3 39.6 1.0 CD2 A:HIS116 4.3 38.8 1.0 NE2 A:HIS116 4.3 40.0 1.0 O4 A:PO4316 4.4 48.4 0.5 N A:ASN117 4.4 38.3 1.0 OE2 A:GLU178 4.7 47.3 1.0 NH2 A:ARG63 4.7 38.4 1.0 C A:HIS116 4.9 38.0 1.0 CZ A:ARG63 4.9 38.9 1.0 CB A:GLU24 5.0 40.5 1.0

Zinc binding site 2 out of 2 in the Crystal Structure of Apo-Aspartoacylase From Human Brain


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 Apo-Aspartoacylase From Human Brain within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn314 b:56.2 occ:1.00 OE1 B:GLU24 2.1 40.0 1.0 ND1 B:HIS21 2.1 38.2 1.0 O1 B:PO4315 2.2 38.8 0.5 ND1 B:HIS116 2.2 35.6 1.0 P B:PO4315 2.7 41.8 0.5 CE1 B:HIS21 2.8 38.4 1.0 O3 B:PO4315 2.9 39.4 0.5 CD B:GLU24 2.9 39.0 1.0 O2 B:PO4315 2.9 43.2 0.5 OE2 B:GLU24 3.0 38.7 1.0 CE1 B:HIS116 3.1 35.4 1.0 CG B:HIS116 3.3 33.7 1.0 CG B:HIS21 3.3 37.3 1.0 CB B:HIS116 3.6 33.2 1.0 CB B:HIS21 3.9 35.6 1.0 NE2 B:HIS21 4.0 38.7 1.0 O4 B:PO4315 4.2 40.5 0.5 NH1 B:ARG63 4.2 35.0 1.0 CD2 B:HIS21 4.3 38.0 1.0 NE2 B:HIS116 4.3 36.2 1.0 CG B:GLU24 4.3 37.9 1.0 O B:ASN117 4.3 33.6 1.0 CD2 B:HIS116 4.4 35.4 1.0 CA B:HIS116 4.4 33.0 1.0 O1 B:PO4316 4.7 47.2 0.5 N B:ASN117 4.7 32.9 1.0 OE2 B:GLU178 5.0 46.6 1.0 NH2 B:ARG63 5.0 35.2 1.0 CZ B:ARG63 5.0 36.1 1.0 CB B:GLU24 5.0 37.9 1.0

J.Le Coq, A.Pavlovsky, R.Malik, R.Sanishvili, C.Xu, R.E.Viola. Examination of the Mechanism of Human Brain Aspartoacylase Through the Binding of An Intermediate Analogue. Biochemistry V. 47 3484 2008.
ISSN: ISSN 0006-2960
PubMed: 18293939
DOI: 10.1021/BI702400X