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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: Thu Oct 17 00:48:49 2024

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