Atomistry » Zinc » PDB 2hpy-2i7v » 2i3c
Atomistry »
  Zinc »
    PDB 2hpy-2i7v »
      2i3c »

Zinc in PDB 2i3c: Crystal Structure of An Aspartoacylase From Homo Sapiens

Enzymatic activity of Crystal Structure of An Aspartoacylase From Homo Sapiens

All present enzymatic activity of Crystal Structure of An Aspartoacylase From Homo Sapiens:
3.5.1.15;

Protein crystallography data

The structure of Crystal Structure of An Aspartoacylase From Homo Sapiens, PDB code: 2i3c was solved by E.Bitto, G.E.Wesenberg, G.N.Phillips Jr., J.G.Mccoy, C.A.Bingman, Centerfor Eukaryotic 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 (%) 19.5 / 24.3

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of An Aspartoacylase From Homo Sapiens (pdb code 2i3c). 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 An Aspartoacylase From Homo Sapiens, PDB code: 2i3c:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 2i3c

Go back to Zinc Binding Sites List in 2i3c
Zinc binding site 1 out of 2 in the 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 Crystal Structure of An Aspartoacylase From Homo Sapiens within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn314

b:41.0
occ:1.00
O2 A:PO4315 1.8 54.2 1.0
OE1 A:GLU24 1.9 49.8 1.0
ND1 A:HIS21 2.0 41.1 1.0
ND1 A:HIS116 2.1 51.2 1.0
OE2 A:GLU24 2.4 54.0 1.0
CD A:GLU24 2.5 51.1 1.0
CE1 A:HIS21 2.8 47.1 1.0
CE1 A:HIS116 2.9 46.8 1.0
P A:PO4315 2.9 62.9 1.0
CG A:HIS21 3.1 40.7 1.0
CG A:HIS116 3.2 47.3 1.0
O3 A:PO4315 3.3 64.2 1.0
O A:HOH329 3.4 38.0 1.0
O4 A:PO4315 3.4 49.3 1.0
CB A:HIS21 3.6 41.1 1.0
CB A:HIS116 3.7 45.2 1.0
NE2 A:HIS21 4.0 40.0 1.0
CG A:GLU24 4.0 44.5 1.0
NE2 A:HIS116 4.1 43.4 1.0
CD2 A:HIS21 4.1 41.4 1.0
O1 A:PO4315 4.2 59.8 1.0
CD2 A:HIS116 4.3 43.4 1.0
O A:ASN117 4.4 46.8 1.0
CA A:HIS116 4.4 45.1 1.0
NH1 A:ARG63 4.4 39.5 1.0
N A:ASN117 4.6 46.0 1.0
CB A:GLU24 4.7 44.2 1.0
N A:HIS21 4.8 44.3 1.0
CA A:HIS21 4.9 42.7 1.0
O1 A:PO4316 4.9 48.2 1.0
NH2 A:ARG63 5.0 36.3 1.0

Zinc binding site 2 out of 2 in 2i3c

Go back to Zinc Binding Sites List in 2i3c
Zinc binding site 2 out of 2 in the 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 Crystal Structure of An Aspartoacylase From Homo Sapiens within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn314

b:41.4
occ:1.00
O3 B:PO4315 1.6 57.7 1.0
OE1 B:GLU24 1.9 48.4 1.0
ND1 B:HIS21 2.0 40.2 1.0
ND1 B:HIS116 2.2 52.6 1.0
CD B:GLU24 2.6 50.4 1.0
OE2 B:GLU24 2.7 51.2 1.0
CE1 B:HIS21 2.9 44.8 1.0
P B:PO4315 2.9 66.2 1.0
CE1 B:HIS116 3.0 48.5 1.0
CG B:HIS21 3.1 42.8 1.0
CG B:HIS116 3.2 49.6 1.0
O2 B:PO4315 3.5 68.2 1.0
O1 B:PO4315 3.6 47.7 1.0
CB B:HIS21 3.6 42.5 1.0
CB B:HIS116 3.6 46.1 1.0
O B:HOH330 3.9 43.6 1.0
O4 B:PO4315 4.0 55.2 1.0
CG B:GLU24 4.0 45.9 1.0
NE2 B:HIS21 4.1 39.8 1.0
NE2 B:HIS116 4.1 45.1 1.0
CD2 B:HIS21 4.2 42.4 1.0
CD2 B:HIS116 4.2 43.5 1.0
NH1 B:ARG63 4.3 38.0 1.0
O B:ASN117 4.3 47.4 1.0
CA B:HIS116 4.4 45.0 1.0
N B:ASN117 4.7 46.0 1.0
CB B:GLU24 4.7 44.5 1.0
N B:HIS21 4.9 44.3 1.0
CA B:HIS21 4.9 42.7 1.0
OE2 B:GLU178 4.9 67.4 1.0

Reference:

E.Bitto, C.A.Bingman, G.E.Wesenberg, J.G.Mccoy, G.N.Phillips. Structure of Aspartoacylase, the Brain Enzyme Impaired in Canavan Disease. Proc.Natl.Acad.Sci.Usa V. 104 456 2007.
ISSN: ISSN 0027-8424
PubMed: 17194761
DOI: 10.1073/PNAS.0607817104
Page generated: Wed Dec 16 03:30:45 2020

Last articles

Zn in 7VD8
Zn in 7V1R
Zn in 7V1Q
Zn in 7VPF
Zn in 7T85
Zn in 7T5F
Zn in 7NF9
Zn in 7M4M
Zn in 7M4O
Zn in 7M4N
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy