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 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