Zinc in PDB 2q51: Ensemble Refinement of the Protein Crystal Structure of An Aspartoacylase From Homo Sapiens

All present enzymatic activity of Ensemble Refinement of the Protein Crystal Structure of An Aspartoacylase From Homo Sapiens:
3.5.1.15;

The structure of Ensemble Refinement of the Protein Crystal Structure of An Aspartoacylase From Homo Sapiens, PDB code: 2q51 was solved by E.J.Levin, D.A.Kondrashov, G.E.Wesenberg, G.N.Phillips Jr., Center Foreukaryotic Structural Genomics (Cesg), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	48.72 / 2.80
Space group	P 42 21 2
Cell size a, b, c (Å), α, β, γ (°)	145.551, 145.551, 103.396, 90.00, 90.00, 90.00
R / Rfree (%)	15.7 / 23.9

The binding sites of Zinc atom in the Ensemble Refinement of the Protein Crystal Structure of An Aspartoacylase From Homo Sapiens (pdb code 2q51). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Ensemble Refinement of the Protein Crystal Structure of An Aspartoacylase From Homo Sapiens, PDB code: 2q51:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Ensemble Refinement of the Protein Crystal Structure of An Aspartoacylase From Homo Sapiens


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Ensemble Refinement of the Protein Crystal Structure of An Aspartoacylase From Homo Sapiens within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn314 b:22.1 occ:0.06 ND1 A:HIS21 2.5 33.9 0.1 OE2 A:GLU24 2.6 38.6 0.1 OE1 A:GLU24 2.6 36.9 0.1 CD A:GLU24 2.8 37.5 0.1 CE1 A:HIS21 3.0 33.3 0.1 ND1 A:HIS116 3.0 35.8 0.1 NH1 A:ARG63 3.4 37.4 0.1 CG A:HIS21 3.8 34.5 0.1 CG A:HIS116 3.8 37.4 0.1 CE1 A:HIS116 3.9 36.7 0.1 O A:ASN117 3.9 39.8 0.1 CB A:HIS116 4.0 38.4 0.1 CG A:GLU24 4.1 37.8 0.1 NE2 A:HIS21 4.2 34.1 0.1 OE2 A:GLU178 4.4 52.5 0.1 CB A:HIS21 4.4 36.0 0.1 O1 A:PO4316 4.4 42.1 0.1 OH A:TYR288 4.5 72.3 0.1 CZ A:ARG63 4.6 35.5 0.1 CD2 A:HIS21 4.6 34.6 0.1 N A:ASN117 4.7 41.0 0.1 CD A:GLU178 4.7 50.5 0.1 C A:ASN117 4.8 39.3 0.1 O A:HOH329 4.9 34.5 0.1 CD2 A:HIS116 4.9 36.5 0.1 NE2 A:HIS116 4.9 35.4 0.1

Zinc binding site 2 out of 2 in the Ensemble Refinement of the Protein Crystal Structure of An Aspartoacylase From Homo Sapiens


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Ensemble Refinement of the Protein Crystal Structure of An Aspartoacylase From Homo Sapiens within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn314 b:30.2 occ:0.06 OE2 B:GLU24 2.1 38.6 0.1 ND1 B:HIS21 2.1 34.7 0.1 ND1 B:HIS116 2.2 37.4 0.1 OE1 B:GLU24 2.4 38.2 0.1 CD B:GLU24 2.5 38.2 0.1 O3 B:PO4315 2.6 40.7 0.1 CE1 B:HIS21 3.0 34.4 0.1 CG B:HIS21 3.1 34.9 0.1 CE1 B:HIS116 3.1 36.8 0.1 CG B:HIS116 3.2 37.2 0.1 CB B:HIS21 3.5 35.0 0.1 CB B:HIS116 3.6 35.3 0.1 OE2 B:GLU178 3.9 51.1 0.1 P B:PO4315 4.0 41.6 0.1 CG B:GLU24 4.0 36.8 0.1 NE2 B:HIS21 4.1 33.3 0.1 CD2 B:HIS21 4.2 34.9 0.1 NH1 B:ARG63 4.2 34.6 0.1 NE2 B:HIS116 4.2 36.4 0.1 NH2 B:ARG63 4.3 31.8 0.1 CD2 B:HIS116 4.3 37.3 0.1 CA B:HIS116 4.4 35.9 0.1 O2 B:PO4315 4.6 42.4 0.1 O B:HOH330 4.6 55.2 0.1 CZ B:ARG63 4.6 35.0 0.1 O1 B:PO4315 4.7 40.6 0.1 O B:ASN117 4.8 38.4 0.1 CA B:HIS21 4.8 36.1 0.1 O4 B:PO4315 4.9 43.1 0.1 N B:HIS21 4.9 35.1 0.1 CB B:GLU24 4.9 36.3 0.1

E.J.Levin, D.A.Kondrashov, G.E.Wesenberg, G.N.Phillips. Ensemble Refinement of Protein Crystal Structures: Validation and Application. Structure V. 15 1040 2007.
ISSN: ISSN 0969-2126
PubMed: 17850744
DOI: 10.1016/J.STR.2007.06.019