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Zinc in PDB 2q4z: Ensemble Refinement of the Protein Crystal Structure of An Aspartoacylase From Rattus Norvegicus

Enzymatic activity of Ensemble Refinement of the Protein Crystal Structure of An Aspartoacylase From Rattus Norvegicus

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

Protein crystallography data

The structure of Ensemble Refinement of the Protein Crystal Structure of An Aspartoacylase From Rattus Norvegicus, PDB code: 2q4z 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) 40.50 / 1.80
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 92.581, 135.778, 54.033, 90.00, 101.49, 90.00
R / Rfree (%) 13.8 / 19.1

Zinc Binding Sites:

The binding sites of Zinc atom in the Ensemble Refinement of the Protein Crystal Structure of An Aspartoacylase From Rattus Norvegicus (pdb code 2q4z). 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 Rattus Norvegicus, PDB code: 2q4z:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 2q4z

Go back to Zinc Binding Sites List in 2q4z
Zinc binding site 1 out of 2 in the Ensemble Refinement of the Protein Crystal Structure of An Aspartoacylase From Rattus Norvegicus


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 Rattus Norvegicus within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn601

b:24.4
occ:0.06
O A:HOH748 2.0 35.6 0.1
O A:HOH778 2.6 27.8 0.1
ND1 A:HIS115 3.1 14.2 0.1
OE2 A:GLU23 3.1 10.6 0.1
OE1 A:GLU23 3.5 12.1 0.1
ND1 A:HIS20 3.6 9.3 0.1
CE1 A:HIS20 3.7 9.6 0.1
CD A:GLU23 3.7 10.5 0.1
CG A:HIS115 3.7 11.9 0.1
CB A:HIS115 3.8 10.6 0.1
CE1 A:HIS115 3.9 16.0 0.1
OE1 A:GLU177 4.0 21.8 0.1
O A:HOH739 4.1 29.4 0.1
O A:ASN116 4.3 9.4 0.1
O A:HOH987 4.4 54.4 0.1
NH1 A:ARG62 4.6 12.9 0.1
CG A:HIS20 4.6 9.6 0.1
NE2 A:HIS20 4.7 9.0 0.1
CD2 A:HIS115 4.8 12.7 0.1
O A:HOH915 4.8 25.7 0.1
NE2 A:HIS115 4.9 13.7 0.1
CA A:HIS115 5.0 10.4 0.1
CD A:GLU177 5.0 22.3 0.1

Zinc binding site 2 out of 2 in 2q4z

Go back to Zinc Binding Sites List in 2q4z
Zinc binding site 2 out of 2 in the Ensemble Refinement of the Protein Crystal Structure of An Aspartoacylase From Rattus Norvegicus


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 Rattus Norvegicus within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn602

b:14.2
occ:0.06
ND1 B:HIS20 2.3 11.4 0.1
OE2 B:GLU23 2.4 7.0 0.1
O B:HOH733 2.7 33.7 0.1
OE1 B:GLU23 2.8 6.5 0.1
CD B:GLU23 2.9 9.5 0.1
CE1 B:HIS20 2.9 13.2 0.1
NH1 B:ARG62 3.0 16.2 0.1
O B:HOH759 3.3 26.0 0.1
ND1 B:HIS115 3.4 15.6 0.1
CG B:HIS20 3.4 12.9 0.1
O3 B:SO4704 3.8 51.4 0.1
CB B:HIS20 4.0 12.6 0.1
O B:HOH716 4.0 16.6 0.1
CZ B:ARG62 4.1 17.8 0.1
CE1 B:HIS115 4.1 15.9 0.1
NE2 B:HIS20 4.2 11.0 0.1
CG B:HIS115 4.3 14.7 0.1
CG B:GLU23 4.3 6.6 0.1
NH2 B:ARG62 4.3 16.8 0.1
CD2 B:HIS20 4.4 11.2 0.1
CB B:HIS115 4.5 12.4 0.1
O B:ASN116 4.5 8.9 0.1
O B:HOH722 4.7 13.7 0.1
S B:SO4704 5.0 51.9 0.1

Reference:

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
Page generated: Wed Dec 16 03:49:59 2020

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