Atomistry » Tin » PDB 3e94-7axg » 6zjc
Atomistry »
  Tin »
    PDB 3e94-7axg »
      6zjc »

Tin in PDB 6zjc: Crystal Structure of Equus Ferus Caballus Glutathione Transferase A3-3 in Complex with Glutathione and Triethyltin

Enzymatic activity of Crystal Structure of Equus Ferus Caballus Glutathione Transferase A3-3 in Complex with Glutathione and Triethyltin

All present enzymatic activity of Crystal Structure of Equus Ferus Caballus Glutathione Transferase A3-3 in Complex with Glutathione and Triethyltin:
2.5.1.18;

Protein crystallography data

The structure of Crystal Structure of Equus Ferus Caballus Glutathione Transferase A3-3 in Complex with Glutathione and Triethyltin, PDB code: 6zjc was solved by J.Skerlova, A.Ismail, H.Lindstrom, B.Sjodin, B.Mannervik, P.Stenmark, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 48.37 / 2.20
Space group P 1
Cell size a, b, c (Å), α, β, γ (°) 49.401, 54.728, 97.115, 88.17, 78.74, 86.39
R / Rfree (%) 17.3 / 21

Tin Binding Sites:

The binding sites of Tin atom in the Crystal Structure of Equus Ferus Caballus Glutathione Transferase A3-3 in Complex with Glutathione and Triethyltin (pdb code 6zjc). This binding sites where shown within 5.0 Angstroms radius around Tin atom.
In total 4 binding sites of Tin where determined in the Crystal Structure of Equus Ferus Caballus Glutathione Transferase A3-3 in Complex with Glutathione and Triethyltin, PDB code: 6zjc:
Jump to Tin binding site number: 1; 2; 3; 4;

Tin binding site 1 out of 4 in 6zjc

Go back to Tin Binding Sites List in 6zjc
Tin binding site 1 out of 4 in the Crystal Structure of Equus Ferus Caballus Glutathione Transferase A3-3 in Complex with Glutathione and Triethyltin


Mono view


Stereo pair view

A full contact list of Tin with other atoms in the Sn binding site number 1 of Crystal Structure of Equus Ferus Caballus Glutathione Transferase A3-3 in Complex with Glutathione and Triethyltin within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Sn302

b:31.2
occ:1.00
SN1 B:QLT302 0.0 31.2 1.0
C04 B:QLT302 2.1 29.5 1.0
C06 B:QLT302 2.1 30.1 1.0
C02 B:QLT302 2.2 23.3 1.0
OH B:TYR9 2.2 23.0 1.0
SG2 B:GSH301 2.3 29.7 1.0
C01 B:QLT302 2.8 21.6 1.0
C05 B:QLT302 3.0 30.7 1.0
C07 B:QLT302 3.1 27.6 1.0
CZ B:TYR9 3.3 22.3 1.0
CB2 B:GSH301 3.3 27.6 1.0
CE1 B:TYR9 3.9 26.8 1.0
CE2 B:TYR9 4.2 23.9 1.0
CG B:ARG15 4.5 21.1 1.0
N B:ARG15 4.5 24.7 1.0
CA2 B:GSH301 4.6 28.2 1.0
CA B:GLY14 4.6 24.8 1.0
CD B:ARG15 5.0 21.7 1.0

Tin binding site 2 out of 4 in 6zjc

Go back to Tin Binding Sites List in 6zjc
Tin binding site 2 out of 4 in the Crystal Structure of Equus Ferus Caballus Glutathione Transferase A3-3 in Complex with Glutathione and Triethyltin


Mono view


Stereo pair view

A full contact list of Tin with other atoms in the Sn binding site number 2 of Crystal Structure of Equus Ferus Caballus Glutathione Transferase A3-3 in Complex with Glutathione and Triethyltin within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Sn302

b:29.0
occ:1.00
SN1 A:QLT302 0.0 29.0 1.0
OH A:TYR9 2.1 28.8 1.0
C06 A:QLT302 2.1 30.3 1.0
C04 A:QLT302 2.1 27.2 1.0
C02 A:QLT302 2.2 23.4 1.0
SG2 A:GSH301 2.4 26.5 1.0
C01 A:QLT302 2.8 23.3 1.0
C05 A:QLT302 3.0 29.5 1.0
C07 A:QLT302 3.1 29.4 1.0
CZ A:TYR9 3.2 25.4 1.0
CB2 A:GSH301 3.3 27.2 1.0
CE1 A:TYR9 3.8 27.1 1.0
CE2 A:TYR9 4.1 24.8 1.0
CG A:ARG15 4.3 20.0 1.0
N A:ARG15 4.4 20.7 1.0
CA2 A:GSH301 4.6 24.1 1.0
CA A:GLY14 4.7 23.9 1.0
CB A:ARG15 4.9 20.1 1.0
CD A:ARG15 5.0 21.5 1.0

Tin binding site 3 out of 4 in 6zjc

Go back to Tin Binding Sites List in 6zjc
Tin binding site 3 out of 4 in the Crystal Structure of Equus Ferus Caballus Glutathione Transferase A3-3 in Complex with Glutathione and Triethyltin


Mono view


Stereo pair view

A full contact list of Tin with other atoms in the Sn binding site number 3 of Crystal Structure of Equus Ferus Caballus Glutathione Transferase A3-3 in Complex with Glutathione and Triethyltin within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Sn302

b:30.6
occ:1.00
SN1 D:QLT302 0.0 30.6 1.0
C06 D:QLT302 2.1 25.4 1.0
C04 D:QLT302 2.1 31.9 1.0
OH D:TYR9 2.1 20.6 1.0
C02 D:QLT302 2.2 29.3 1.0
SG2 D:GSH301 2.4 29.1 1.0
C01 D:QLT302 2.9 31.4 1.0
C07 D:QLT302 2.9 27.4 1.0
C05 D:QLT302 3.0 32.3 1.0
CZ D:TYR9 3.2 23.1 1.0
CB2 D:GSH301 3.3 28.1 1.0
CE1 D:TYR9 3.9 21.6 1.0
CE2 D:TYR9 4.1 21.7 1.0
CG D:ARG15 4.4 22.7 1.0
N D:ARG15 4.5 24.9 1.0
CA2 D:GSH301 4.6 26.5 1.0
CA D:GLY14 4.7 26.3 1.0
CB D:ARG15 5.0 22.2 1.0
CD D:ARG15 5.0 27.6 1.0
CE2 D:PHE222 5.0 94.7 1.0

Tin binding site 4 out of 4 in 6zjc

Go back to Tin Binding Sites List in 6zjc
Tin binding site 4 out of 4 in the Crystal Structure of Equus Ferus Caballus Glutathione Transferase A3-3 in Complex with Glutathione and Triethyltin


Mono view


Stereo pair view

A full contact list of Tin with other atoms in the Sn binding site number 4 of Crystal Structure of Equus Ferus Caballus Glutathione Transferase A3-3 in Complex with Glutathione and Triethyltin within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Sn302

b:30.2
occ:1.00
SN1 C:QLT302 0.0 30.2 1.0
C06 C:QLT302 2.1 33.7 1.0
C04 C:QLT302 2.1 28.7 1.0
OH C:TYR9 2.2 24.4 1.0
C02 C:QLT302 2.2 23.6 1.0
SG2 C:GSH301 2.4 30.0 1.0
C01 C:QLT302 2.9 19.4 1.0
C07 C:QLT302 3.0 39.6 1.0
C05 C:QLT302 3.0 30.2 1.0
CZ C:TYR9 3.3 23.9 1.0
CB2 C:GSH301 3.3 29.6 1.0
CE1 C:TYR9 3.9 26.7 1.0
CE2 C:TYR9 4.2 25.9 1.0
CG C:ARG15 4.5 22.3 1.0
N C:ARG15 4.5 24.0 1.0
CA2 C:GSH301 4.6 28.0 1.0
CA C:GLY14 4.6 24.8 1.0
O C:HOH459 4.8 39.0 1.0
CB C:ARG15 5.0 21.4 1.0
CD C:ARG15 5.0 23.4 1.0

Reference:

J.Skerlova, A.Ismail, H.Lindstrom, B.Sjodin, B.Mannervik, P.Stenmark. Structural and Functional Analysis of the Inhibition of Equine Glutathione Transferase A3-3 By Organotin Endocrine Disrupting Pollutants. Environ Pollut 15960 2020.
ISSN: ISSN 1873-6424
PubMed: 33162212
DOI: 10.1016/J.ENVPOL.2020.115960
Page generated: Wed Dec 16 02:10:24 2020

Last articles

Zn in 7NA9
Zn in 7LZP
Zn in 7M1H
Zn in 7L6V
Zn in 7CM0
V in 7P8R
Ni in 7L19
Na in 7T88
Na in 7MJ5
Na in 7L00
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy