Calcium in PDB 3csh: Crystal Structure of Glutathione Transferase Pi in Complex with the Chlorambucil-Glutathione Conjugate

Enzymatic activity of Crystal Structure of Glutathione Transferase Pi in Complex with the Chlorambucil-Glutathione Conjugate

All present enzymatic activity of Crystal Structure of Glutathione Transferase Pi in Complex with the Chlorambucil-Glutathione Conjugate:
2.5.1.18;

Protein crystallography data

The structure of Crystal Structure of Glutathione Transferase Pi in Complex with the Chlorambucil-Glutathione Conjugate, PDB code: 3csh 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)*	18.69 / 1.55
*Space group*	C 1 2 1
*Cell size a, b, c (Å), α, β, γ (°)*	77.346, 89.358, 68.946, 90.00, 98.03, 90.00
*R / R_free (%)*	17 / 20

Other elements in 3csh:

The structure of Crystal Structure of Glutathione Transferase Pi in Complex with the Chlorambucil-Glutathione Conjugate also contains other interesting chemical elements:

Chlorine

(Cl)

4 atoms

Calcium Binding Sites:

The binding sites of Calcium atom in the Crystal Structure of Glutathione Transferase Pi in Complex with the Chlorambucil-Glutathione Conjugate (pdb code 3csh). 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 Glutathione Transferase Pi in Complex with the Chlorambucil-Glutathione Conjugate, PDB code: 3csh:

Calcium binding site 1 out of 1 in 3csh

Go back to

Calcium Binding Sites List in 3csh

Calcium binding site 1 out of 1 in the Crystal Structure of Glutathione Transferase Pi in Complex with the Chlorambucil-Glutathione Conjugate

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 Glutathione Transferase Pi in Complex with the Chlorambucil-Glutathione Conjugate within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
B:Ca210 b:11.2 occ:0.50	O	B:HOH478	2.3	18.2	1.0
	O	B:HOH561	2.3	28.8	1.0
	O	B:GLY77	2.4	12.8	1.0
	OE1	B:GLN147	2.4	23.3	1.0
	O	B:HOH544	2.4	25.3	1.0
	O	B:HOH538	2.4	31.1	1.0
	O	B:HOH512	2.7	20.5	1.0
	C	B:GLY77	3.6	13.1	1.0
	CD	B:GLN147	3.6	22.2	1.0
	CB	B:GLN147	4.2	14.8	1.0
	CA	B:GLY77	4.3	12.5	1.0
	O	B:HOH458	4.4	24.4	1.0
	CD2	B:LEU78	4.4	13.6	1.0
	CG	B:GLN147	4.5	17.5	1.0
	O	B:HOH501	4.5	21.6	1.0
	NE2	B:GLN147	4.5	24.7	1.0
	N	B:LEU78	4.6	11.7	1.0
	O	B:ILE148	4.7	11.7	1.0
	O	B:HOH411	4.7	15.2	1.0
	O	B:LEU76	4.7	14.2	1.0
	O	B:HOH415	4.7	14.7	1.0
	CA	B:LEU78	4.8	11.4	1.0
	O	B:HOH468	4.8	36.3	1.0

Reference:

L.J.Parker, S.Ciccone, L.C.Italiano, A.Primavera, A.J.Oakley, C.J.Morton, N.C.Hancock, M.L.Bello, M.W.Parker. The Anti-Cancer Drug Chlorambucil As A Substrate For the Human Polymorphic Enzyme Glutathione Transferase P1-1: Kinetic Properties and Crystallographic Characterisation of Allelic Variants. J.Mol.Biol. V. 380 131 2008.
ISSN: ISSN 0022-2836
PubMed: 18511072
DOI: 10.1016/J.JMB.2008.04.066

Page generated: Sat Jul 13 08:45:51 2024

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