Atomistry » Chlorine » PDB 5imx-5ivr » 5in2
Atomistry »
  Chlorine »
    PDB 5imx-5ivr »
      5in2 »

Chlorine in PDB 5in2: Crystal Structure of Extra Cellular Cu/Zn Superoxide Dismutase From Onchocerca Volvulus at 1.5 Angstrom; Insight Into Novel Binding Site and New Inhibitors

Enzymatic activity of Crystal Structure of Extra Cellular Cu/Zn Superoxide Dismutase From Onchocerca Volvulus at 1.5 Angstrom; Insight Into Novel Binding Site and New Inhibitors

All present enzymatic activity of Crystal Structure of Extra Cellular Cu/Zn Superoxide Dismutase From Onchocerca Volvulus at 1.5 Angstrom; Insight Into Novel Binding Site and New Inhibitors:
1.15.1.1;

Protein crystallography data

The structure of Crystal Structure of Extra Cellular Cu/Zn Superoxide Dismutase From Onchocerca Volvulus at 1.5 Angstrom; Insight Into Novel Binding Site and New Inhibitors, PDB code: 5in2 was solved by A.Moustafa, C.Betzel, M.Perbandt, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 25.29 / 1.55
Space group P 31 2 1
Cell size a, b, c (Å), α, β, γ (°) 58.410, 58.410, 77.630, 90.00, 90.00, 120.00
R / Rfree (%) 16 / 18.1

Other elements in 5in2:

The structure of Crystal Structure of Extra Cellular Cu/Zn Superoxide Dismutase From Onchocerca Volvulus at 1.5 Angstrom; Insight Into Novel Binding Site and New Inhibitors also contains other interesting chemical elements:

Zinc (Zn) 1 atom
Copper (Cu) 1 atom

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of Extra Cellular Cu/Zn Superoxide Dismutase From Onchocerca Volvulus at 1.5 Angstrom; Insight Into Novel Binding Site and New Inhibitors (pdb code 5in2). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the Crystal Structure of Extra Cellular Cu/Zn Superoxide Dismutase From Onchocerca Volvulus at 1.5 Angstrom; Insight Into Novel Binding Site and New Inhibitors, PDB code: 5in2:

Chlorine binding site 1 out of 1 in 5in2

Go back to Chlorine Binding Sites List in 5in2
Chlorine binding site 1 out of 1 in the Crystal Structure of Extra Cellular Cu/Zn Superoxide Dismutase From Onchocerca Volvulus at 1.5 Angstrom; Insight Into Novel Binding Site and New Inhibitors


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure of Extra Cellular Cu/Zn Superoxide Dismutase From Onchocerca Volvulus at 1.5 Angstrom; Insight Into Novel Binding Site and New Inhibitors within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl205

b:66.6
occ:1.00
 H A:SER27 2.4 88.8 1.0
HG22 A:ILE28 2.6 76.1 1.0
H A:ILE28 2.8 51.2 1.0
HB2 A:SER27 2.9 86.5 1.0
N A:SER27 3.2 74.0 1.0
HA3 A:GLY23 3.3 75.9 1.0
O A:SER24 3.4 84.4 1.0
CG2 A:ILE28 3.5 63.4 1.0
N A:ILE28 3.5 42.7 1.0
CB A:SER27 3.7 72.1 1.0
HG23 A:ILE28 3.8 76.1 1.0
CA A:SER27 3.9 74.4 1.0
HG21 A:ILE28 4.0 76.1 1.0
H A:GLY23 4.0 63.5 1.0
N A:GLY26 4.0 84.0 1.0
CA A:GLY23 4.0 63.2 1.0
H A:GLY26 4.1 0.8 1.0
C A:GLY23 4.1 62.5 1.0
HB3 A:SER27 4.2 86.5 1.0
O A:GLY23 4.2 59.1 1.0
C A:SER27 4.2 61.9 1.0
C A:GLY25 4.3 83.4 1.0
C A:GLY26 4.3 80.5 1.0
HA2 A:GLY26 4.3 97.1 1.0
C A:SER24 4.4 78.8 1.0
CA A:GLY26 4.4 80.9 1.0
O A:ILE28 4.4 36.5 1.0
CB A:ILE28 4.4 43.6 1.0
N A:GLY23 4.4 52.9 1.0
HB A:ILE28 4.5 52.3 1.0
HA3 A:GLY25 4.5 97.9 1.0
CA A:ILE28 4.5 39.0 1.0
O A:GLY25 4.5 84.1 1.0
OG A:SER27 4.7 81.7 1.0
N A:SER24 4.8 68.4 1.0
HA A:SER27 4.8 89.3 1.0
CA A:GLY25 4.8 81.5 1.0
HA2 A:GLY23 4.8 75.9 1.0
HG A:SER27 4.9 98.0 1.0
C A:ILE28 5.0 37.1 1.0

Reference:

A.Moustafa, C.Betzel, M.Perbandt. Crystal Structure of Extracellular Cu/Zn Superoxide Dismutase From Onchocerca Volvulus at 1.5 Angstrom; Insight Into Novel Binding Site and New Inhibitors To Be Published.
Page generated: Fri Jul 26 09:30:17 2024

Last articles

Zn in 9MJ5
Zn in 9HNW
Zn in 9G0L
Zn in 9FNE
Zn in 9DZN
Zn in 9E0I
Zn in 9D32
Zn in 9DAK
Zn in 8ZXC
Zn in 8ZUF
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy