Atomistry » Zinc » PDB 4hwr-4i7c » 4hzt
Atomistry »
  Zinc »
    PDB 4hwr-4i7c »
      4hzt »

Zinc in PDB 4hzt: Structure-Based Design of Novel Dihydroisoquinoline Bace-1 Inhibitors That Do Not Engage the Catalytic Aspartates

Enzymatic activity of Structure-Based Design of Novel Dihydroisoquinoline Bace-1 Inhibitors That Do Not Engage the Catalytic Aspartates

All present enzymatic activity of Structure-Based Design of Novel Dihydroisoquinoline Bace-1 Inhibitors That Do Not Engage the Catalytic Aspartates:
3.4.23.46;

Protein crystallography data

The structure of Structure-Based Design of Novel Dihydroisoquinoline Bace-1 Inhibitors That Do Not Engage the Catalytic Aspartates, PDB code: 4hzt was solved by N.Yao, E.Brecht, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 60.00 / 1.80
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 75.256, 103.972, 100.302, 90.00, 90.00, 90.00
R / Rfree (%) 19.8 / 25.6

Other elements in 4hzt:

The structure of Structure-Based Design of Novel Dihydroisoquinoline Bace-1 Inhibitors That Do Not Engage the Catalytic Aspartates also contains other interesting chemical elements:

Chlorine (Cl) 1 atom

Zinc Binding Sites:

The binding sites of Zinc atom in the Structure-Based Design of Novel Dihydroisoquinoline Bace-1 Inhibitors That Do Not Engage the Catalytic Aspartates (pdb code 4hzt). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 3 binding sites of Zinc where determined in the Structure-Based Design of Novel Dihydroisoquinoline Bace-1 Inhibitors That Do Not Engage the Catalytic Aspartates, PDB code: 4hzt:
Jump to Zinc binding site number: 1; 2; 3;

Zinc binding site 1 out of 3 in 4hzt

Go back to Zinc Binding Sites List in 4hzt
Zinc binding site 1 out of 3 in the Structure-Based Design of Novel Dihydroisoquinoline Bace-1 Inhibitors That Do Not Engage the Catalytic Aspartates


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structure-Based Design of Novel Dihydroisoquinoline Bace-1 Inhibitors That Do Not Engage the Catalytic Aspartates within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn501

b:27.5
occ:1.00
ND1 A:HIS457 1.9 24.2 1.0
NE2 A:HIS459 2.0 28.0 1.0
CE1 A:HIS459 2.9 30.5 1.0
CE1 A:HIS457 2.9 28.3 1.0
CG A:HIS457 2.9 30.6 1.0
CD2 A:HIS459 3.1 27.4 1.0
CB A:HIS457 3.3 30.9 1.0
NE2 A:HIS457 4.0 25.9 1.0
CD2 A:HIS457 4.0 26.9 1.0
ND1 A:HIS459 4.0 27.4 1.0
CG A:HIS459 4.2 29.8 1.0
CA A:HIS457 4.9 31.6 1.0

Zinc binding site 2 out of 3 in 4hzt

Go back to Zinc Binding Sites List in 4hzt
Zinc binding site 2 out of 3 in the Structure-Based Design of Novel Dihydroisoquinoline Bace-1 Inhibitors That Do Not Engage the Catalytic Aspartates


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Structure-Based Design of Novel Dihydroisoquinoline Bace-1 Inhibitors That Do Not Engage the Catalytic Aspartates within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn502

b:40.4
occ:1.00
O A:HOH729 2.2 38.3 1.0
ND1 A:HIS458 2.2 44.3 1.0
NE2 A:HIS460 2.2 39.5 1.0
OD1 A:ASP192 2.4 30.0 1.0
OD2 A:ASP192 2.4 32.8 1.0
CG A:ASP192 2.7 28.2 1.0
CE1 A:HIS460 2.8 43.6 1.0
O A:HOH628 3.0 47.5 1.0
CG A:HIS458 3.0 38.1 1.0
CE1 A:HIS458 3.1 44.0 1.0
CB A:HIS458 3.3 34.1 1.0
CD2 A:HIS460 3.4 44.3 1.0
CA A:HIS458 3.6 33.5 1.0
ND1 A:HIS460 4.1 46.1 1.0
CD2 A:HIS458 4.1 41.8 1.0
NE2 A:HIS458 4.1 41.6 1.0
CB A:ASP192 4.2 26.9 1.0
O A:HIS457 4.3 31.9 1.0
CG A:HIS460 4.4 42.8 1.0
O A:HOH745 4.5 31.9 1.0
C A:HIS458 4.6 32.7 1.0
N A:HIS458 4.6 32.4 1.0
O A:HOH839 4.9 57.0 1.0
C A:HIS457 4.9 32.6 1.0

Zinc binding site 3 out of 3 in 4hzt

Go back to Zinc Binding Sites List in 4hzt
Zinc binding site 3 out of 3 in the Structure-Based Design of Novel Dihydroisoquinoline Bace-1 Inhibitors That Do Not Engage the Catalytic Aspartates


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Structure-Based Design of Novel Dihydroisoquinoline Bace-1 Inhibitors That Do Not Engage the Catalytic Aspartates within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn503

b:33.0
occ:1.00
NE2 A:HIS150 2.1 24.0 1.0
OE2 A:GLU78 2.3 30.4 1.0
CD2 A:HIS150 2.9 25.3 1.0
CE1 A:HIS150 3.1 26.6 1.0
CD A:GLU78 3.2 34.6 1.0
OE1 A:GLU78 3.6 38.4 1.0
CG A:HIS150 4.1 25.6 1.0
ND1 A:HIS150 4.1 26.3 1.0
O A:HOH801 4.2 44.3 1.0
CG A:GLU78 4.5 26.5 1.0
CB A:PRO149 4.7 25.7 1.0
CB A:GLU78 4.8 23.2 1.0
CG A:PRO149 5.0 26.7 1.0

Reference:

S.Bowers, Y.Z.Xu, S.Yuan, G.D.Probst, R.K.Hom, W.Chan, A.W.Konradi, H.L.Sham, Y.L.Zhu, P.Beroza, H.Pan, E.Brecht, N.Yao, J.Lougheed, D.Tam, Z.Ren, L.Ruslim, M.P.Bova, D.R.Artis. Structure-Based Design of Novel Dihydroisoquinoline Bace-1 Inhibitors That Do Not Engage the Catalytic Aspartates. Bioorg.Med.Chem.Lett. V. 23 2181 2013.
ISSN: ISSN 0960-894X
PubMed: 23465612
DOI: 10.1016/J.BMCL.2013.01.103
Page generated: Wed Dec 16 05:23:04 2020

Last articles

Zn in 8WB0
Zn in 8WAX
Zn in 8WAU
Zn in 8WAZ
Zn in 8WAY
Zn in 8WAV
Zn in 8WAW
Zn in 8WAT
Zn in 8W7M
Zn in 8WD3
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy