Calcium in PDB 2a2s: Crystal Structure of Human Glutathione Transferase in Complex with S-Nitrosoglutathione in the Absence of Reducing Agent

Enzymatic activity of Crystal Structure of Human Glutathione Transferase in Complex with S-Nitrosoglutathione in the Absence of Reducing Agent

All present enzymatic activity of Crystal Structure of Human Glutathione Transferase in Complex with S-Nitrosoglutathione in the Absence of Reducing Agent:
2.5.1.18;

Protein crystallography data

The structure of Crystal Structure of Human Glutathione Transferase in Complex with S-Nitrosoglutathione in the Absence of Reducing Agent, PDB code: 2a2s was solved by L.J.Parker, C.J.Morton, J.J.Adams, M.W.Parker, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

*Resolution Low / High (Å)*	30.00 / 1.70
*Space group*	C 1 2 1
*Cell size a, b, c (Å), α, β, γ (°)*	77.640, 89.640, 68.850, 90.00, 97.98, 90.00
*R / R_free (%)*	17.8 / 20.8

Calcium Binding Sites:

The binding sites of Calcium atom in the Crystal Structure of Human Glutathione Transferase in Complex with S-Nitrosoglutathione in the Absence of Reducing Agent (pdb code 2a2s). 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 Human Glutathione Transferase in Complex with S-Nitrosoglutathione in the Absence of Reducing Agent, PDB code: 2a2s:

Calcium binding site 1 out of 1 in 2a2s

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Calcium Binding Sites List in 2a2s

Calcium binding site 1 out of 1 in the Crystal Structure of Human Glutathione Transferase in Complex with S-Nitrosoglutathione in the Absence of Reducing Agent

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 Human Glutathione Transferase in Complex with S-Nitrosoglutathione in the Absence of Reducing Agent within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
B:Ca210 b:17.1 occ:0.93	O	B:HOH2304	2.3	14.0	1.0
	O	B:HOH2325	2.4	20.4	1.0
	O	B:HOH2346	2.4	22.2	1.0
	OE1	B:GLN147	2.4	21.2	1.0
	O	B:GLY77	2.5	11.9	1.0
	O	B:HOH2382	2.5	31.4	1.0
	O	B:HOH2281	2.7	18.9	1.0
	CD	B:GLN147	3.6	29.5	1.0
	C	B:GLY77	3.7	11.0	1.0
	CB	B:GLN147	4.3	13.9	1.0
	O	B:HOH2442	4.4	21.4	1.0
	CA	B:GLY77	4.4	11.4	1.0
	CG	B:GLN147	4.5	24.4	1.0
	NE2	B:GLN147	4.5	29.4	1.0
	CD2	B:LEU78	4.5	14.6	1.0
	O	B:HOH2247	4.6	14.9	1.0
	O	B:HOH2335	4.6	24.0	1.0
	N	B:LEU78	4.6	10.9	1.0
	O	B:HOH2316	4.7	24.6	1.0
	O	B:HOH2230	4.7	14.8	1.0
	O	B:ILE148	4.7	10.9	1.0
	CA	B:LEU78	4.8	10.0	1.0
	O	B:LEU76	4.8	15.5	1.0

Reference:

R.Tellez-Sanz, E.Cesareo, M.Nuccetelli, A.M.Aguilera, C.Baron, L.J.Parker, J.J.Adams, C.J.Morton, M.Lo Bello, M.W.Parker, L.Garcia-Fuentes. Calorimetric and Structural Studies of the Nitric Oxide Carrier S-Nitrosoglutathione Bound to Human Glutathione Transferase P1-1 Protein Sci. V. 15 1093 2006.
ISSN: ISSN 0961-8368
PubMed: 16597834
DOI: 10.1110/PS.052055206

Page generated: Fri Jul 12 08:31:07 2024

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