Atomistry » Cadmium » PDB 1a4k-1dmf » 1aw9
Atomistry »
  Cadmium »
    PDB 1a4k-1dmf »
      1aw9 »

Cadmium in PDB 1aw9: Structure of Glutathione S-Transferase III in Apo Form

Enzymatic activity of Structure of Glutathione S-Transferase III in Apo Form

All present enzymatic activity of Structure of Glutathione S-Transferase III in Apo Form:
2.5.1.18;

Protein crystallography data

The structure of Structure of Glutathione S-Transferase III in Apo Form, PDB code: 1aw9 was solved by T.Neuefeind, R.Huber, P.Reinemer, J.Knaeblein, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 8.00 / 2.20
Space group P 63 2 2
Cell size a, b, c (Å), α, β, γ (°) 97.770, 97.770, 116.450, 90.00, 90.00, 120.00
R / Rfree (%) 19.7 / n/a

Cadmium Binding Sites:

The binding sites of Cadmium atom in the Structure of Glutathione S-Transferase III in Apo Form (pdb code 1aw9). This binding sites where shown within 5.0 Angstroms radius around Cadmium atom.
In total 5 binding sites of Cadmium where determined in the Structure of Glutathione S-Transferase III in Apo Form, PDB code: 1aw9:
Jump to Cadmium binding site number: 1; 2; 3; 4; 5;

Cadmium binding site 1 out of 5 in 1aw9

Go back to Cadmium Binding Sites List in 1aw9
Cadmium binding site 1 out of 5 in the Structure of Glutathione S-Transferase III in Apo Form


Mono view


Stereo pair view

A full contact list of Cadmium with other atoms in the Cd binding site number 1 of Structure of Glutathione S-Transferase III in Apo Form within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cd219

b:34.7
occ:1.00
HD1 A:HIS150 1.5 0.0 1.0
H2 A:HOH385 1.6 0.0 1.0
O A:HOH385 1.8 25.2 1.0
ND1 A:HIS150 2.4 16.4 1.0
H1 A:HOH385 2.6 0.0 1.0
H2 A:HOH331 2.8 0.0 1.0
O A:HOH331 2.9 30.8 1.0
O A:HOH276 2.9 29.0 1.0
CE1 A:HIS150 3.1 16.4 1.0
CG A:HIS150 3.5 15.1 1.0
H1 A:HOH276 3.5 0.0 1.0
H1 A:HOH331 3.6 0.0 1.0
H2 A:HOH276 3.7 0.0 1.0
HH21 A:ARG153 3.8 0.0 1.0
O A:HOH314 3.9 35.8 1.0
HD21 A:ASN154 3.9 0.0 1.0
CB A:HIS150 4.0 16.2 1.0
HE1 A:TRP99 4.0 0.0 1.0
H1 A:HOH314 4.1 0.0 1.0
NE2 A:HIS150 4.3 15.0 1.0
CA A:HIS150 4.4 16.7 1.0
HD22 A:ASN154 4.4 0.0 1.0
ND2 A:ASN154 4.4 20.7 1.0
H2 A:HOH314 4.5 0.0 1.0
CD2 A:HIS150 4.5 14.9 1.0
CZ2 A:TRP99 4.5 16.4 1.0
HE A:ARG153 4.6 0.0 1.0
NH2 A:ARG153 4.7 53.9 1.0
NE1 A:TRP99 4.8 17.0 1.0

Cadmium binding site 2 out of 5 in 1aw9

Go back to Cadmium Binding Sites List in 1aw9
Cadmium binding site 2 out of 5 in the Structure of Glutathione S-Transferase III in Apo Form


Mono view


Stereo pair view

A full contact list of Cadmium with other atoms in the Cd binding site number 2 of Structure of Glutathione S-Transferase III in Apo Form within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cd220

b:3.2
occ:0.50
CE1 A:HIS190 2.7 23.2 1.0
ND1 A:HIS190 3.5 23.3 1.0
HD1 A:HIS190 3.5 0.0 1.0
NE2 A:HIS190 3.7 22.5 1.0
HE2 A:HIS190 3.8 0.0 1.0
O A:HOH354 4.3 47.3 1.0
H2 A:HOH387 4.4 0.0 1.0
H2 A:HOH354 4.4 0.0 1.0
O A:ALA152 4.5 26.5 1.0
CG A:HIS190 4.8 19.4 1.0
O A:HOH387 4.8 49.1 1.0
CA A:ALA152 4.8 24.3 1.0
CD2 A:HIS190 4.9 20.3 1.0
H2 A:HOH335 4.9 0.0 1.0
O A:HOH335 4.9 36.7 1.0

Cadmium binding site 3 out of 5 in 1aw9

Go back to Cadmium Binding Sites List in 1aw9
Cadmium binding site 3 out of 5 in the Structure of Glutathione S-Transferase III in Apo Form


Mono view


Stereo pair view

A full contact list of Cadmium with other atoms in the Cd binding site number 3 of Structure of Glutathione S-Transferase III in Apo Form within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cd222

b:49.0
occ:1.00
OE2 A:GLU138 2.5 33.9 1.0
H2 A:HOH380 2.5 0.0 1.0
OE1 A:GLU138 2.7 30.7 1.0
CD A:GLU138 2.9 25.8 1.0
O A:HOH380 3.2 57.5 1.0
H2 A:HOH312 3.3 0.0 1.0
H1 A:HOH380 3.7 0.0 1.0
O A:HOH312 4.1 33.9 1.0
H1 A:HOH320 4.2 0.0 1.0
H1 A:HOH251 4.2 0.0 1.0
CG A:GLU138 4.3 20.3 1.0
O A:HOH320 4.6 67.6 1.0
H1 A:HOH312 4.8 0.0 1.0
H2 A:HOH251 4.8 0.0 1.0

Cadmium binding site 4 out of 5 in 1aw9

Go back to Cadmium Binding Sites List in 1aw9
Cadmium binding site 4 out of 5 in the Structure of Glutathione S-Transferase III in Apo Form


Mono view


Stereo pair view

A full contact list of Cadmium with other atoms in the Cd binding site number 4 of Structure of Glutathione S-Transferase III in Apo Form within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cd226

b:46.8
occ:1.00
H1 A:HOH383 2.4 0.0 1.0
CE1 A:HIS106 2.6 20.4 1.0
O A:HOH383 3.2 50.2 1.0
HE2 A:HIS106 3.3 0.0 1.0
NE2 A:HIS106 3.3 18.5 1.0
H2 A:HOH383 3.3 0.0 1.0
ND1 A:HIS106 3.6 16.7 1.0
HD1 A:HIS106 3.9 0.0 1.0
H1 A:HOH256 3.9 0.0 1.0
CB A:HIS105 4.0 19.5 1.0
CD2 A:HIS106 4.5 17.6 1.0
CG A:HIS105 4.6 28.6 1.0
CG A:HIS106 4.6 15.2 1.0
CD2 A:HIS105 4.7 31.1 1.0
H1 A:HOH232 4.8 0.0 1.0
O A:HOH256 4.8 21.3 1.0
H2 A:HOH256 4.9 0.0 1.0

Cadmium binding site 5 out of 5 in 1aw9

Go back to Cadmium Binding Sites List in 1aw9
Cadmium binding site 5 out of 5 in the Structure of Glutathione S-Transferase III in Apo Form


Mono view


Stereo pair view

A full contact list of Cadmium with other atoms in the Cd binding site number 5 of Structure of Glutathione S-Transferase III in Apo Form within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cd376

b:52.6
occ:1.00
OD2 A:ASP28 2.5 46.9 1.0
CG A:ASP28 3.3 41.7 1.0
OD1 A:ASP28 3.4 43.5 1.0
CB A:ASP28 4.6 36.8 1.0

Reference:

T.Neuefeind, R.Huber, P.Reinemer, J.Knablein, L.Prade, K.Mann, B.Bieseler. Cloning, Sequencing, Crystallization and X-Ray Structure of Glutathione S-Transferase-III From Zea Mays Var. Mutin: A Leading Enzyme in Detoxification of Maize Herbicides. J.Mol.Biol. V. 274 577 1997.
ISSN: ISSN 0022-2836
PubMed: 9417936
DOI: 10.1006/JMBI.1997.1401
Page generated: Sat Dec 12 08:08:26 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