Calcium in PDB 3dgq: Crystal Structure of the Glutathione Transferase Pi Enzyme in Complex with the Bifunctional Inhibitor, Etharapta

Enzymatic activity of Crystal Structure of the Glutathione Transferase Pi Enzyme in Complex with the Bifunctional Inhibitor, Etharapta

All present enzymatic activity of Crystal Structure of the Glutathione Transferase Pi Enzyme in Complex with the Bifunctional Inhibitor, Etharapta:
2.5.1.18;

Protein crystallography data

The structure of Crystal Structure of the Glutathione Transferase Pi Enzyme in Complex with the Bifunctional Inhibitor, Etharapta, PDB code: 3dgq was solved by L.J.Parker, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

*Resolution Low / High (Å)*	19.53 / 1.60
*Space group*	C 1 2 1
*Cell size a, b, c (Å), α, β, γ (°)*	77.930, 90.330, 68.960, 90.00, 98.88, 90.00
*R / R_free (%)*	19.5 / 22.7

Other elements in 3dgq:

The structure of Crystal Structure of the Glutathione Transferase Pi Enzyme in Complex with the Bifunctional Inhibitor, Etharapta also contains other interesting chemical elements:

Chlorine

(Cl)

4 atoms

Calcium Binding Sites:

The binding sites of Calcium atom in the Crystal Structure of the Glutathione Transferase Pi Enzyme in Complex with the Bifunctional Inhibitor, Etharapta (pdb code 3dgq). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total only one binding site of Calcium was determined in the Crystal Structure of the Glutathione Transferase Pi Enzyme in Complex with the Bifunctional Inhibitor, Etharapta, PDB code: 3dgq:

Calcium binding site 1 out of 1 in 3dgq

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Calcium Binding Sites List in 3dgq

Calcium binding site 1 out of 1 in the Crystal Structure of the Glutathione Transferase Pi Enzyme in Complex with the Bifunctional Inhibitor, Etharapta

Mono view

Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Crystal Structure of the Glutathione Transferase Pi Enzyme in Complex with the Bifunctional Inhibitor, Etharapta within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
B:Ca210 b:12.6 occ:0.40	O	B:HOH350	2.3	24.8	1.0
	O	B:HOH387	2.3	26.3	1.0
	O	B:GLY77	2.4	14.5	1.0
	OE1	B:GLN147	2.5	26.3	1.0
	O	B:HOH362	2.5	28.3	1.0
	O	B:HOH472	2.8	39.4	1.0
	O	B:HOH298	2.8	24.7	1.0
	C	B:GLY77	3.6	13.9	1.0
	CD	B:GLN147	3.7	22.4	1.0
	CB	B:GLN147	4.4	17.4	1.0
	CD2	B:LEU78	4.4	15.4	1.0
	CA	B:GLY77	4.4	13.3	1.0
	O	B:HOH349	4.5	29.9	1.0
	NE2	B:GLN147	4.6	24.8	1.0
	O	B:HOH379	4.6	25.9	1.0
	O	B:HOH380	4.6	31.2	1.0
	N	B:LEU78	4.6	12.4	1.0
	CG	B:GLN147	4.6	18.8	1.0
	O	B:LEU76	4.7	15.7	1.0
	O	B:ILE148	4.8	12.4	1.0
	O	B:HOH346	4.8	16.9	1.0
	CA	B:LEU78	4.8	12.3	1.0
	O	B:HOH249	4.9	17.9	1.0

Reference:

W.H.Ang, L.J.Parker, A.De Luca, L.Juillerat-Jeanneret, C.J.Morton, M.Lo Bello, M.W.Parker, P.J.Dyson. Rational Design of An Organometallic Glutathione Transferase Inhibitor Angew.Chem.Int.Ed.Engl. V. 48 3854 2009.
ISSN: ISSN 1433-7851
PubMed: 19396894
DOI: 10.1002/ANIE.200900185

Page generated: Tue Jul 8 11:38:44 2025

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