Cadmium in PDB 1aw9: 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;

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

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 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 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 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 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 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

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