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Chlorine in PDB 1pl1: Crystal Structure of Human Glutathione Transferase (Gst) A1-1 in Complex with A Decarboxy-Glutathione

Enzymatic activity of Crystal Structure of Human Glutathione Transferase (Gst) A1-1 in Complex with A Decarboxy-Glutathione

All present enzymatic activity of Crystal Structure of Human Glutathione Transferase (Gst) A1-1 in Complex with A Decarboxy-Glutathione:
2.5.1.18;

Protein crystallography data

The structure of Crystal Structure of Human Glutathione Transferase (Gst) A1-1 in Complex with A Decarboxy-Glutathione, PDB code: 1pl1 was solved by E.Grahn, E.Jakobsson, A.Gustafsson, L.Grehn, B.Olin, M.Wahlberg, D.Madsen, G.J.Kleywegt, B.Mannervik, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 67.42 / 1.75
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 99.505, 90.247, 51.130, 90.00, 93.67, 90.00
R / Rfree (%) 14.8 / 18.9

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of Human Glutathione Transferase (Gst) A1-1 in Complex with A Decarboxy-Glutathione (pdb code 1pl1). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Crystal Structure of Human Glutathione Transferase (Gst) A1-1 in Complex with A Decarboxy-Glutathione, PDB code: 1pl1:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in 1pl1

Go back to Chlorine Binding Sites List in 1pl1
Chlorine binding site 1 out of 2 in the Crystal Structure of Human Glutathione Transferase (Gst) A1-1 in Complex with A Decarboxy-Glutathione


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 Human Glutathione Transferase (Gst) A1-1 in Complex with A Decarboxy-Glutathione within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl702

b:12.5
occ:1.00
OG1 A:THR68 3.0 15.3 1.0
O A:HOH717 3.2 8.6 1.0
N A:THR68 3.2 7.7 1.0
O A:HOH849 3.3 20.2 1.0
CA1 A:ABY654 3.5 16.6 1.0
CG1 A:ABY654 3.6 14.5 1.0
CD A:PRO56 3.6 8.3 1.0
CB1 A:ABY654 3.7 14.9 1.0
CB A:THR68 3.8 10.0 1.0
CA A:GLN67 3.9 7.3 1.0
C A:GLN67 4.0 7.8 1.0
N1 A:ABY654 4.0 17.8 1.0
CA A:THR68 4.0 9.0 1.0
CD A:ARG15 4.2 10.5 1.0
CG A:PRO56 4.3 9.2 1.0
OE1 A:GLN67 4.3 10.1 1.0
O A:HOH791 4.3 14.1 1.0
N A:GLN67 4.4 7.3 1.0
N A:PRO56 4.5 7.3 1.0
O A:VAL55 4.6 7.0 1.0
CB A:ARG15 4.7 7.5 1.0
O A:HOH725 4.7 12.9 1.0
O A:HOH940 4.8 31.4 1.0
CD1 A:ABY654 4.9 14.8 1.0
C A:VAL55 4.9 6.9 1.0
CB A:PRO56 4.9 7.6 1.0
O A:HOH707 4.9 6.8 1.0
CD A:GLN67 5.0 10.6 1.0
CB A:GLN67 5.0 7.8 1.0

Chlorine binding site 2 out of 2 in 1pl1

Go back to Chlorine Binding Sites List in 1pl1
Chlorine binding site 2 out of 2 in the Crystal Structure of Human Glutathione Transferase (Gst) A1-1 in Complex with A Decarboxy-Glutathione


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Crystal Structure of Human Glutathione Transferase (Gst) A1-1 in Complex with A Decarboxy-Glutathione within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl701

b:11.3
occ:1.00
OG1 B:THR68 3.1 15.9 1.0
O B:HOH706 3.1 7.9 1.0
O B:HOH746 3.2 22.5 1.0
N B:THR68 3.2 8.5 1.0
CA1 B:ABY655 3.5 15.6 1.0
CG1 B:ABY655 3.6 11.8 1.0
CD B:PRO56 3.6 11.3 1.0
CB1 B:ABY655 3.7 13.7 1.0
CB B:THR68 3.8 10.4 1.0
CA B:GLN67 3.9 9.2 1.0
C B:GLN67 4.0 7.6 1.0
CA B:THR68 4.0 8.5 1.0
CD B:ARG15 4.1 11.4 1.0
N1 B:ABY655 4.1 16.4 1.0
CG B:PRO56 4.2 12.0 1.0
OE1 B:GLN67 4.3 11.6 1.0
N B:GLN67 4.4 8.9 1.0
O B:HOH729 4.4 15.4 1.0
N B:PRO56 4.5 10.7 1.0
O B:VAL55 4.6 10.9 1.0
O A:HOH750 4.7 11.0 1.0
CB B:ARG15 4.7 9.2 1.0
CB B:PRO56 4.8 11.3 1.0
CD1 B:ABY655 4.8 10.1 1.0
O B:HOH846 4.8 28.4 1.0
C B:VAL55 4.9 10.7 1.0
CD B:GLN67 5.0 12.3 1.0

Reference:

E.Grahn, M.Novotny, E.Jakobsson, A.Gustafsson, L.Grehn, B.Olin, D.Madsen, M.Wahlberg, B.Mannervik, G.J.Kleywegt. New Crystal Structures of Human Glutathione Transferase A1-1 Shed Light on Glutathione Binding and the Conformation of the C-Terminal Helix. Acta Crystallogr.,Sect.D V. 62 197 2006.
ISSN: ISSN 0907-4449
PubMed: 16421451
DOI: 10.1107/S0907444905039296
Page generated: Sat Dec 12 08:45:58 2020

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