Magnesium in PDB 3nam: Sr Ca(2+)-Atpase in the HNE2 State Complexed with the Thapsigargin Derivative Dotg

Enzymatic activity of Sr Ca(2+)-Atpase in the HNE2 State Complexed with the Thapsigargin Derivative Dotg

All present enzymatic activity of Sr Ca(2+)-Atpase in the HNE2 State Complexed with the Thapsigargin Derivative Dotg:
3.6.3.8;

Protein crystallography data

The structure of Sr Ca(2+)-Atpase in the HNE2 State Complexed with the Thapsigargin Derivative Dotg, PDB code: 3nam was solved by A.M.L.Winther, Y.Sonntag, C.Olesen, J.V.Moller, P.Nissen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

*Resolution Low / High (Å)*	30.00 / 3.10
*Space group*	P 4₁ 2₁ 2
*Cell size a, b, c (Å), α, β, γ (°)*	71.545, 71.545, 591.227, 90.00, 90.00, 90.00
*R / R_free (%)*	23.9 / 28

Other elements in 3nam:

The structure of Sr Ca(2+)-Atpase in the HNE2 State Complexed with the Thapsigargin Derivative Dotg also contains other interesting chemical elements:

Sodium

(Na)

1 atom

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Sr Ca(2+)-Atpase in the HNE2 State Complexed with the Thapsigargin Derivative Dotg (pdb code 3nam). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the Sr Ca(2+)-Atpase in the HNE2 State Complexed with the Thapsigargin Derivative Dotg, PDB code: 3nam:

Magnesium binding site 1 out of 1 in 3nam

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Magnesium Binding Sites List in 3nam

Magnesium binding site 1 out of 1 in the Sr Ca(2+)-Atpase in the HNE2 State Complexed with the Thapsigargin Derivative Dotg

Mono view

Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Sr Ca(2+)-Atpase in the HNE2 State Complexed with the Thapsigargin Derivative Dotg within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
A:Mg996 b:83.0 occ:1.00	O	A:HOH1000	2.5	84.7	1.0
	OD1	A:ASP703	2.6	82.3	1.0
	OD2	A:ASP707	2.8	76.4	1.0
	O	A:HOH1001	3.4	69.2	1.0
	CG	A:ASP707	3.6	74.6	1.0
	CG	A:ASP703	3.7	81.1	1.0
	OD1	A:ASP707	3.8	76.8	1.0
	OD1	A:ASN706	3.8	71.5	1.0
	N	A:GLY704	3.8	77.7	1.0
	OD2	A:ASP703	4.2	80.5	1.0
	CA	A:GLY704	4.2	77.6	1.0
	CA	A:GLY182	4.3	92.0	1.0
	N	A:ASP703	4.6	77.8	1.0
	CG	A:ASN706	4.7	71.3	1.0
	C	A:ASP703	4.8	78.0	1.0
	ND2	A:ASN706	4.8	74.5	1.0
	N	A:GLY182	4.9	88.7	1.0
	CB	A:ASP703	5.0	79.3	1.0
	CB	A:ASP707	5.0	72.0	1.0

Reference:

A.M.L.Winther, H.Liu, Y.Sonntag, C.Olesen, M.Le Maire, H.Soehoel, C.E.Olsen, S.B.Christensen, P.Nissen, J.V.Moller. Critical Roles of Hydrophobicity and Orientation of Side Chains For Inactivation of Sarcoplasmic Reticulum CA2+-Atpase with Thapsigargin and Thapsigargin Analogs J.Biol.Chem. V. 285 28883 2010.
ISSN: ISSN 0021-9258
PubMed: 20551329
DOI: 10.1074/JBC.M110.136242

Page generated: Mon Aug 11 00:51:50 2025

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