Potassium in PDB 3nan: Sr Ca(2+)-Atpase in the HNE2 State Complexed with A Thapsigargin Derivative Boc-(Phi)Tg

Enzymatic activity of Sr Ca(2+)-Atpase in the HNE2 State Complexed with A Thapsigargin Derivative Boc-(Phi)Tg

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

Protein crystallography data

The structure of Sr Ca(2+)-Atpase in the HNE2 State Complexed with A Thapsigargin Derivative Boc-(Phi)Tg, PDB code: 3nan 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)*	45.00 / 3.10
*Space group*	P 4₁ 2₁ 2
*Cell size a, b, c (Å), α, β, γ (°)*	71.330, 71.330, 589.210, 90.00, 90.00, 90.00
*R / R_free (%)*	24.2 / 27.7

Other elements in 3nan:

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

Magnesium

(Mg)

1 atom

Potassium Binding Sites:

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

Potassium binding site 1 out of 1 in 3nan

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Potassium Binding Sites List in 3nan

Potassium binding site 1 out of 1 in the Sr Ca(2+)-Atpase in the HNE2 State Complexed with A Thapsigargin Derivative Boc-(Phi)Tg

Mono view

Stereo pair view

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

probe	atom	residue	distance (Å)	B	Occ
A:K995 b:91.0 occ:1.00	O	A:LYS712	3.1	62.3	1.0
	O	A:ALA714	3.2	65.0	1.0
	OE2	A:GLU732	3.3	65.0	1.0
	C	A:LYS712	3.5	63.1	1.0
	OE1	A:GLU732	3.5	64.4	1.0
	CD	A:GLU732	3.7	65.4	1.0
	O	A:LEU711	3.7	64.8	1.0
	CA	A:LYS712	3.8	64.0	1.0
	OE1	A:GLN244	4.3	96.3	1.0
	N	A:LYS713	4.3	63.0	1.0
	O	A:GLU715	4.3	63.9	1.0
	C	A:ALA714	4.4	65.7	1.0
	C	A:LEU711	4.6	62.9	1.0
	CG	A:LYS712	4.7	69.5	1.0
	N	A:LYS712	4.7	63.7	1.0
	N	A:ALA714	4.7	66.2	1.0
	CB	A:GLN244	4.7	90.2	1.0
	C	A:LYS713	4.8	65.7	1.0
	C	A:GLU715	4.8	65.1	1.0
	O	A:ALA730	4.8	60.5	1.0
	CA	A:LYS713	4.8	64.5	1.0
	CB	A:LYS712	4.9	65.9	1.0
	CD	A:GLN244	4.9	95.2	1.0
	CG	A:GLU732	4.9	62.6	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 12 08:50:09 2024

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